RsiV

• Description: anti-sigma factor to SigV
  
  

Gene name	rsiV
Synonyms	yrhM
Essential	no
Product	anti-sigma factor to SigV
Function	control of SigV activity
Gene expression levels in SubtiExpress: rsiV
Interactions involving this protein in SubtInteract: RsiV
MW, pI	32 kDa, 5.833
Gene length, protein length	855 bp, 285 aa
Immediate neighbours	sigV, oatA
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

sigma factors and their control, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigV regulon

The gene

Basic information

• Locus tag: BSU27130

Database entries

• BsubCyc: BSU27130

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:
  • upon exposure to lysozyme, the extracellular domain of RsiV is cleaved off by an unknown protease, subsequently the N-terminal part of the protein is subject to intramemrane proteolysis by RasP PubMed

• Interactions:
  • SigV-RsiV, this interaction inhibits the activity of SigV PubMed
  • RasP-RsiV, degradation of RsiV PubMed

• Localization:
  • membrane PubMed

Database entries

• BsubCyc: BSU27130

• Structure:

• UniProt: O05403

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sigV-rsiV-oatA-yrhK PubMed

• Expression browser: rsiV PubMed

• Sigma factor: SigV PubMed

• Regulation:
  • induced by lysozyme (SigV) PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Jessica L Hastie, Kyle B Williams, Craig D Ellermeier
The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV.
J Bacteriol: 2013, 195(14);3135-44
[PubMed:23687273] [WorldCat.org] [DOI] (I p)

Yun Luo, Kei Asai, Yoshito Sadaie, John D Helmann
Transcriptomic and phenotypic characterization of a Bacillus subtilis strain without extracytoplasmic function σ factors.
J Bacteriol: 2010, 192(21);5736-45
[PubMed:20817771] [WorldCat.org] [DOI] (I p)

Stephan Zellmeier, Claudia Hofmann, Sylvia Thomas, Thomas Wiegert, Wolfgang Schumann
Identification of sigma(V)-dependent genes of Bacillus subtilis.
FEMS Microbiol Lett: 2005, 253(2);221-9
[PubMed:16274938] [WorldCat.org] [DOI] (P p)

Mika Yoshimura, Kei Asai, Yoshito Sadaie, Hirofumi Yoshikawa
Interaction of Bacillus subtilis extracytoplasmic function (ECF) sigma factors with the N-terminal regions of their potential anti-sigma factors.
Microbiology (Reading): 2004, 150(Pt 3);591-599
[PubMed:14993308] [WorldCat.org] [DOI] (P p)