Difference between revisions of "RsbT"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot) |
* '''Protein family:''' | * '''Protein family:''' |
Revision as of 12:34, 23 May 2009
- Description: PP2C activator, protein serine kinase, phosphorylates RsbS, part of the stressosome
Gene name | rsbT |
Synonyms | ycxT |
Essential | no |
Product | PP2C activator, protein serine kinase |
Function | control of SigB activity |
MW, pI | 14 kDa, 6.587 |
Gene length, protein length | 399 bp, 133 aa |
Immediate neighbours | rsbS, rsbU |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure: 3VY9 (complete stressosome)
- Swiss prot entry: P42411
- KEGG entry: BSU04690
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
- Marles-Wright, J., Grant, T., Delumeau, O., van Duinen, G., Firbank, S. J., Lewis, P. J., Murray, J. W., Newman, J. A., Quin, M. B., Race, P. R., Rohou, A., Tichelaar, W., van Heel, M. & Lewis, R. J. (2008) Molecular architecture of the "stressosome," a signal integration and transduction hub. Science 322: 92-96. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed