RasP

• 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 DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, proteolysis, sigma factors and their control, membrane proteins

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]

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:

• Interactions:
  • RasP-FtsL, RasP-RsiW

• Localization: cell membrane PubMed

Database entries

• Structure:

• UniProt: O31754

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: rasP PubMed

• Sigma factor:

• 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

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)