Difference between revisions of "RasP"
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|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"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU16560 rasP] |
|- | |- | ||
|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] | |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] | ||
| Line 24: | Line 24: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ispC]]'', ''[[proS]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ispC]]'', ''[[proS]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU16560 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU16560 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU16560 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:yluC_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:yluC_context.gif]] | ||
Revision as of 12:51, 13 May 2013
- Description: intramembrane protease, cleaves FtsL and RsiW as well as signal peptides after release of the secreted proteins
| Gene name | rasP |
| Synonyms | yluC |
| Essential | no |
| Product | intramembrane protease |
| Function | control of cell division and SigW activity |
| Gene expression levels in SubtiExpress: rasP | |
| 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 |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
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
- defects in competence development, protein secretion and membrane protein production PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 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
Additional reviews: PubMed
Gu Chen, Xu Zhang
New insights into S2P signaling cascades: regulation, variation, and conservation.
Protein Sci: 2010, 19(11);2015-30
[PubMed:20836086]
[WorldCat.org]
[DOI]
(I p)
Original Publications
Additional original publications: PubMed
Akira Saito, Yohei Hizukuri, Ei-ichi Matsuo, Shinobu Chiba, Hiroyuki Mori, Osamu Nishimura, Koreaki Ito, Yoshinori Akiyama
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria.
Proc Natl Acad Sci U S A: 2011, 108(33);13740-5
[PubMed:21810987]
[WorldCat.org]
[DOI]
(I p)
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)
