PP2C activator, protein serine kinase, phosphorylates RsbS and RsbR, part of the stressosome
function
control of SigB activity
product
PP2C activator, protein serine kinase
Genomic Context
categories
[category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.4|Protein modification] → [category|SW 3.3.4.2|Protein kinases][category|SW 3|Information processing] → [category|SW 3.4|Regulation of gene expression] → [category|SW 3.4.1|Sigma factors and their control] → [category|SW 3.4.1.2|Control of sigma factors][SW|Categories] containing this gene/protein
[SW|protein modification], [SW|sigma factors and their control]Gene
Coordinates on the chromosome (coding sequence)
520,606 -> 521,007
The protein
Catalyzed reaction/ biological activity
phosphorylation of [protein|search|RsbR], [SW|RsbRB], [SW|RsbRC], and [SW|RsbRD] [Pubmed|21362065]Effectors of protein activity
phosphorylated [protein|search|RsbR] activates the kinase activity of [protein|search|RsbT] [Pubmed|23320651]activity is stimulated by light in a [protein|search|YtvA]-dependent manner [Pubmed|23416074]Structure
[PDB|3VY9] (complete stressosome)[SW|Interactions]
[protein|search|RsbS]-[protein|search|RsbT] [Pubmed|16321960][protein|search|RsbR]-[protein|search|RsbT] [Pubmed|21362065][SW|RsbRB]-[protein|search|RsbT] [Pubmed|21362065][SW|RsbRC]-[protein|search|RsbT] [Pubmed|21362065][SW|RsbRD]-[protein|search|RsbT] [Pubmed|21362065][protein|search|RsbT]-[protein|search|RsbU]component of the [SW|stressosome]Expression and Regulation
Operon
''[protein|search|rsbR]-[protein|search|rsbS]-[protein|search|rsbT]-[protein|search|rsbU]-[protein|search|rsbV]-[protein|search|rsbW]-[protein|search|sigB]-[protein|search|rsbX]'' [Pubmed|8002610][SW|Sigma factor]
[protein|search|SigA] [Pubmed|8002610]Regulation
constitutively expressed [Pubmed|20019076]Additional information
[protein|search|RsbT] is synthesized at the same rate as [protein|search|RsbRA] and [protein|search|RsbS], however, the [protein|search|RsbT] level in growing 'B. subtilis' is only 10% that of [protein|search|RsbRA], suggesting that the protein is unstable [PubMed|20019076].Labs working on this gene/protein
[SW|Bill Haldenwang], San Antonio, USA[SW|Chet Price], Davis, USA [http://foodscience.ucdavis.edu/price_lab/pricelab.html homepage][SW|Rick Lewis], Newcastle, UK [http://www.ncl.ac.uk/camb/staff/profile/r.lewis homepage]References
Reviews
19704888,16319496,20658979 Original Articles
8682789,8002610,8682769,9658013,17303566,9786195,15090521,10781545,15583165,8824586,10329124,16321960,8808936,15312768,11244072,15342582,20019076,12499568,12950928,16321960,8955331,18832644,24599254,23407164,23320651,21362065,23416074,21979936 
