RasP
- Description: intramembrane protease, cleaves FtsL, RsiV 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 SigV 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 |
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
- mutants grow slower in liquid, are not competent, can’t activate SigW, have cell division defects, and decreased long term survival PubMed
Database entries
- BsubCyc: BSU16560
- 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
- BsubCyc: BSU16560
- Structure:
- UniProt: O31754
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 24 PubMed
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
Noël Molière, Kürşad Turgay
General and regulatory proteolysis in Bacillus subtilis.
Subcell Biochem: 2013, 66;73-103
[PubMed:23479438]
[WorldCat.org]
[DOI]
(P p)
Ross E Dalbey, Peng Wang, Jan Maarten van Dijl
Membrane proteases in the bacterial protein secretion and quality control pathway.
Microbiol Mol Biol Rev: 2012, 76(2);311-30
[PubMed:22688815]
[WorldCat.org]
[DOI]
(I p)
Theresa D Ho, Craig D Ellermeier
Extra cytoplasmic function σ factor activation.
Curr Opin Microbiol: 2012, 15(2);182-8
[PubMed:22381678]
[WorldCat.org]
[DOI]
(I p)
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)
Michael S Wolfe
Intramembrane-cleaving proteases.
J Biol Chem: 2009, 284(21);13969-73
[PubMed:19189971]
[WorldCat.org]
[DOI]
(P p)
Original publications