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P54504 (RSBRD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RsbT co-antagonist protein RsbRD
Alternative name(s):
Stressosome protein RsbRD
Gene names
Name:rsbRD
Synonyms:yqhA
Ordered Locus Names:BSU24760
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. Ref.4 Ref.5

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. Ref.4 Ref.5

Subunit structure

Probably present in the stressosome with RsbRA, RsbRB, RsbRC and RsbS. Ref.5

Post-translational modification

Phosphorylated by RsbT. Ref.4

Disruption phenotype

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. Ref.4

Sequence similarities

Contains 1 STAS domain.

Ontologies

Keywords
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278RsbT co-antagonist protein RsbRD
PRO_0000049817

Regions

Domain160 – 271112STAS

Amino acid modifications

Modified residue1811Phosphothreonine Ref.6

Experimental info

Sequence conflict401E → G in BAA12530. Ref.1
Sequence conflict891V → F in BAA12530. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54504 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: B5057DE23E0914D7

FASTA27831,835
        10         20         30         40         50         60 
MIALDQHLTE HKKDITQQWL EVCTSNGSWL YSAKDQQKLE QKLKDQHELL VTIVAKSLRK 

        70         80         90        100        110        120 
EDVEDELNRW SLQCARDRAV HEVTVTQSVG QFNTFRHIMF EWIHKFSEAS SQDISIQEFY 

       130        140        150        160        170        180 
EWSRILNQNI DEIIEVFTEE YHQVTMIQLN AQKEMINELS APIMPITDGI GILPLVGEID 

       190        200        210        220        230        240 
THRARTILES VLEQCSALKL SYLFLDISGV PIVDTMVAYQ IFKVIDSTKL LGIETIISGI 

       250        260        270 
RPEIAQTVVK LGLDFSNVKT EQSLAKALAN KGFKIKEC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84432 Genomic DNA. Translation: BAA12530.1.
AL009126 Genomic DNA. Translation: CAB14407.2.
PIRD69958.
RefSeqNP_390356.2. NC_000964.3.

3D structure databases

ProteinModelPortalP54504.
SMRP54504. Positions 162-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU24760.

PTM databases

PhosSiteP0712194.

Proteomic databases

PaxDbP54504.

Protocols and materials databases

DNASU938513.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14407; CAB14407; BSU24760.
GeneID938513.
KEGGbsu:BSU24760.
PATRIC18976786. VBIBacSub10457_2583.

Organism-specific databases

GenoListBSU24760. [Micado]

Phylogenomic databases

eggNOGCOG1366.
HOGENOMHOG000008785.
KOK17763.
OrthoDBEOG6G4VQG.
PhylomeDBP54504.

Enzyme and pathway databases

BioCycBSUB:BSU24760-MONOMER.

Family and domain databases

Gene3D3.30.750.24. 1 hit.
InterProIPR025751. RsbRD_N_dom.
IPR002645. STAS_dom.
[Graphical view]
PfamPF14361. RsbRD_N. 1 hit.
PF01740. STAS. 1 hit.
[Graphical view]
SUPFAMSSF52091. SSF52091. 1 hit.
PROSITEPS50801. STAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRSBRD_BACSU
AccessionPrimary (citable) accession number: P54504
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList