Difference between revisions of "CssS"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
+ | ** the extracellular loop domain is required for signal perception {{PubMed|22307758}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
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** [[CssS]]-[[CssR]] | ** [[CssS]]-[[CssR]] | ||
− | * '''[[Localization]]:''' cell membrane (according to Swiss-Prot) | + | * '''[[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|22307758}} | ||
=== Database entries === | === Database entries === | ||
Line 136: | Line 139: | ||
=References= | =References= | ||
− | <pubmed>10094672,17600057,21630458,17088376,12270824,11555295, 19820159 21602801 21624103</pubmed> | + | <pubmed>10094672,17600057,21630458,17088376,12270824,11555295, 19820159 21602801 21624103 22307758</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:28, 13 February 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 This image was kindly provided by SubtiList
|
Contents
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
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
- Interactions:
- CssS is a member of a suspected group of hubs proteins that were suggested to be involved in a large number of interactions PubMed
- CssS-CssR
- 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:
- UniProt: O32193
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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)