Difference between revisions of "CssR"

From SubtiWiki
Jump to: navigation, search
(The protein)
Line 66: Line 66:
 
* '''Domains:'''  
 
* '''Domains:'''  
  
* '''Modification:'''
+
* '''Modification:''' phosphorylated by [[CssS]] on an Asp residue
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
* '''Effectors of protein activity:'''
+
* '''Effectors of protein activity:''' phosphorylation likely affects DNA-binding activity
  
* '''Interactions:'''
+
* '''Interactions:''' [[CssS]]-[[CssR]]
  
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)

Revision as of 19:09, 30 November 2009

  • Description: two-component response regulator, control of cellular responses to protein secretion stress

Gene name cssR
Synonyms yvqA
Essential no
Product two-component response regulator
Function control of cellular responses to protein secretion stress
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 26 kDa, 5.071
Gene length, protein length 675 bp, 225 aa
Immediate neighbours htrB, cssS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CssR context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU33010

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: OmpR family of two-component response regulators
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated by CssS on an Asp residue
  • Cofactor(s):
  • Effectors of protein activity: phosphorylation likely affects DNA-binding activity
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • expressed under conditions of secretion stress (CssR) PubMed
  • 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

Jessica C Zweers, Thomas Wiegert, Jan Maarten van Dijl
Stress-responsive systems set specific limits to the overproduction of membrane proteins in Bacillus subtilis.
Appl Environ Microbiol: 2009, 75(23);7356-64
[PubMed:19820159] [WorldCat.org] [DOI] (I p)

Hanne-Leena Hyyryläinen, Milla Pietiäinen, Tuula Lundén, Anna Ekman, Marika Gardemeister, Sanna Murtomäki-Repo, Haike Antelmann, Michael Hecker, Leena Valmu, Matti Sarvas, Vesa P Kontinen
The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 7);2126-2136
[PubMed:17600057] [WorldCat.org] [DOI] (P p)

Elise Darmon, Ronald Dorenbos, Jochen Meens, Roland Freudl, Haike Antelmann, Michael Hecker, Oscar P Kuipers, Sierd Bron, Wim J Quax, Jean-Yves F Dubois, Jan Maarten van Dijl
A disulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus subtilis.
Appl Environ Microbiol: 2006, 72(11);6876-85
[PubMed:17088376] [WorldCat.org] [DOI] (P p)

Elise Darmon, David Noone, Anne Masson, Sierd Bron, Oscar P Kuipers, Kevin M Devine, Jan Maarten van Dijl
A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis.
J Bacteriol: 2002, 184(20);5661-71
[PubMed:12270824] [WorldCat.org] [DOI] (P p)

H L Hyyryläinen, A Bolhuis, E Darmon, L Muukkonen, P Koski, M Vitikainen, M Sarvas, Z Prágai, S Bron, J M van Dijl, V P Kontinen
A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress.
Mol Microbiol: 2001, 41(5);1159-72
[PubMed:11555295] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)