Difference between revisions of "RasP"
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|style="background:#ABCDEF;" align="center"| '''Product''' || intramembrane protease | |style="background:#ABCDEF;" align="center"| '''Product''' || intramembrane protease | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || control of cell division and [[SigW]] activity | + | |style="background:#ABCDEF;" align="center"|'''Function''' || control of [[cell division]] and [[SigW]] activity |
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/RasP RasP] | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 5.14 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 5.14 |
Revision as of 08:40, 28 July 2011
Gene name | rasP |
Synonyms | yluC |
Essential | no |
Product | intramembrane protease |
Function | control of cell division and SigW activity |
Interactions involving this protein in SubtInteract: RasP | |
MW, pI | 46 kDa, 5.14 |
Gene length, protein length | 1266 bp, 422 aa |
Immediate neighbours | ispC, proS |
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
cell division, proteolysis, sigma factors and their control, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU16560
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Protein family: peptidase M50B family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane PubMed
Database entries
- Structure:
- UniProt: O31754
- KEGG entry: [2]
- 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
Thomas Wiegert, University of Bayreuth, Germany Homepage
Your additional remarks
References
Reviews
Original Publications
Inga Wadenpohl, Marc Bramkamp
DivIC stabilizes FtsL against RasP cleavage.
J Bacteriol: 2010, 192(19);5260-3
[PubMed:20644139]
[WorldCat.org]
[DOI]
(I p)
Janine Heinrich, Kerstin Hein, Thomas Wiegert
Two proteolytic modules are involved in regulated intramembrane proteolysis of Bacillus subtilis RsiW.
Mol Microbiol: 2009, 74(6);1412-26
[PubMed:19889088]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Janine Heinrich, Tuula Lundén, Vesa P Kontinen, Thomas Wiegert
The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP.
Microbiology (Reading): 2008, 154(Pt 7);1989-1997
[PubMed:18599827]
[WorldCat.org]
[DOI]
(P p)
Marc Bramkamp, Louise Weston, Richard A Daniel, Jeff Errington
Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis.
Mol Microbiol: 2006, 62(2);580-91
[PubMed:17020588]
[WorldCat.org]
[DOI]
(P p)
Stephan Zellmeier, Wolfgang Schumann, Thomas Wiegert
Involvement of Clp protease activity in modulating the Bacillus subtilissigmaw stress response.
Mol Microbiol: 2006, 61(6);1569-82
[PubMed:16899079]
[WorldCat.org]
[DOI]
(P p)
Susanne Schöbel, Stephan Zellmeier, Wolfgang Schumann, Thomas Wiegert
The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC.
Mol Microbiol: 2004, 52(4);1091-105
[PubMed:15130127]
[WorldCat.org]
[DOI]
(P p)