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://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU16560 rasP]
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|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]
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ispC]]'', ''[[proS]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ispC]]'', ''[[proS]]''
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13529&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|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
YluC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RasP expression.png















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

  • Catalyzed reaction/ biological activity:
    • cleaves FtsL and RsiW
    • cleaves signal peptides after release of the secreted proteins PubMed
  • 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:

Database entries

  • Structure:
  • 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)