P54504 (RSBRD_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: RsbT co-antagonist protein RsbRD Alternative name(s): Stressosome protein RsbRD | ||||||
| Gene names |
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| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 278 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
|---|---|
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| None. [Check GOA] | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 278 | 278 | RsbT co-antagonist protein RsbRD | PRO_0000049817 | |||||
Regions | |||||||||
| Domain | 160 – 271 | 112 | STAS | ||||||
Amino acid modifications | |||||||||
| Modified residue | 181 | 1 | Phosphothreonine Ref.6 | ||||||
Experimental info | |||||||||
| Sequence conflict | 40 | 1 | E → G in BAA12530. Ref.1 | ||||||
| Sequence conflict | 89 | 1 | V → F in BAA12530. Ref.1 | ||||||
Sequences
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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. 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, MASS SPECTROMETRY. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D84432 Genomic DNA. Translation: BAA12530.1. AL009126 Genomic DNA. Translation: CAB14407.2. |
| PIR | D69958. |
| RefSeq | NP_390356.2. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P54504. |
| SMR | P54504. Positions 162-276. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU24760. |
PTM databases | |
| PhosSite | P0712194. |
Proteomic databases | |
| PaxDb | P54504. |
Protocols and materials databases | |
| DNASU | 938513. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB14407; CAB14407; BSU24760. |
| GeneID | 938513. |
| KEGG | bsu:BSU24760. |
| PATRIC | 18976786. VBIBacSub10457_2583. |
Organism-specific databases | |
| GenoList | BSU24760. [Micado] |
Phylogenomic databases | |
| eggNOG | COG1366. |
| HOGENOM | HOG000008785. |
| ProtClustDB | CLSK887569. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU24760-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.750.24. 1 hit. |
| InterPro | IPR025751. RsbRD_N_dom. IPR002645. STAS_dom. [Graphical view] |
| Pfam | PF14361. RsbRD_N. 1 hit. PF01740. STAS. 1 hit. [Graphical view] |
| SUPFAM | SSF52091. STAS. 1 hit. |
| PROSITE | PS50801. STAS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RSBRD_BACSU | ||||||||
| Accession | Primary (citable) accession number: P54504 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
