Difference between revisions of "CssS"

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|colspan="2" | '''Genetic context''' <br/> [[Image:cssS_context.gif]]
 
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cssS_3386398_3387753_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:cssS_expression.png|500px]]
 
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Revision as of 08:53, 23 April 2012

  • Description: two-component sensor kinase, control of cellular responses to protein secretion stress

Gene name cssS
Synonyms yvqB
Essential no
Product two-component sensor kinase
Function control of cellular responses to protein secretion stress
Interactions involving this protein in SubtInteract: CssS
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 51 kDa, 5.795
Gene length, protein length 1353 bp, 451 aa
Immediate neighbours cssR, yirB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CssS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CssS expression.png




























Categories containing this gene/protein

protein modification, transcription factors and their control, heat shock proteins, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CssR regulon

The gene

Basic information

  • Locus tag: BSU33020

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of CssR
  • Protein family:

Extended information on the protein

  • Kinetic information:
  • Domains: two transmembrane segments, C-terminal histidine phosphotransferase domain
  • Modification: autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity:
    • the extracellular loop domain is required for signal perception PubMed
  • Localization:
    • cell membrane (according to Swiss-Prot)
    • localized primarily at the division septum but also found in a punctate pattern with lower intensity throughout the cell cylinder PubMed

Database entries

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

Additional information

Expression and regulation

  • 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

David Noone, Eric Botella, Clodagh Butler, Annette Hansen, Inga Jende, Kevin M Devine
Signal perception by the secretion stress-responsive CssRS two-component system in Bacillus subtilis.
J Bacteriol: 2012, 194(7);1800-14
[PubMed:22307758] [WorldCat.org] [DOI] (I p)

Elodie Marchadier, Rut Carballido-López, Sophie Brinster, Céline Fabret, Peggy Mervelet, Philippe Bessières, Marie-Françoise Noirot-Gros, Vincent Fromion, Philippe Noirot
An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach.
Proteomics: 2011, 11(15);2981-91
[PubMed:21630458] [WorldCat.org] [DOI] (I p)

Hein Trip, Patricia J van der Veek, Ton C Renniers, Rob Meima, Cees M Sagt, Lisette Mohrmann, Oscar P Kuipers
A novel screening system for secretion of heterologous proteins in Bacillus subtilis.
Microb Biotechnol: 2011, 4(5);673-82
[PubMed:21624103] [WorldCat.org] [DOI] (I p)

Des Raj Kashyap, Minhui Wang, Li-Hui Liu, Geert-Jan Boons, Dipika Gupta, Roman Dziarski
Peptidoglycan recognition proteins kill bacteria by activating protein-sensing two-component systems.
Nat Med: 2011, 17(6);676-83
[PubMed:21602801] [WorldCat.org] [DOI] (I p)

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)