Difference between revisions of "SpoIVA"

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* '''Additional information:'''
 
* '''Additional information:'''
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 276 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 10 {{PubMed|21395229}}
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** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 309 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:14, 17 April 2014

  • Description: ATPase, spore coat morphogenetic protein, anchors the spore coat to the spore surface via SpoVM

Gene name spoIVA
Synonyms spoVP
Essential no
Product ATPase, basement layer protein for spore coat assembly
Function spore cortex formation and coat assembly
Gene expression levels in SubtiExpress: spoIVA
Interactions involving this protein in SubtInteract: SpoIVA
MW, pI 55 kDa, 4.546
Gene length, protein length 1476 bp, 492 aa
Immediate neighbours hbs, yphF
Sequences Protein DNA DNA_with_flanks
Genetic context
SpoIVA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SpoIVA expression.png















Categories containing this gene/protein

sporulation proteins

This gene is a member of the following regulons

SigE regulon, SpoIIID regulon

SpoIVA-dependent proteins of the spore coat basement

The gene

Basic information

  • Locus tag: BSU22800

Phenotypes of a mutant

  • the spore coat does not localize to the spore surface but self-assembles into aggregates in the mother cell cytoplasm PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • uses ATP hydrolysis to drive self-assembly into static filaments PubMed
    • ATP hydrolysis drives polymerization of a nucleotide-free filament PubMed
    • ploymerization depends on a critical threshold concentration of SpoIVA that is only achieved once the protein is recruited to the surface of the developing spore PubMed
  • Protein family:
    • belongs to the TRAFAC class of P-loop GTPases, but has lost the ability to bind GTP PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: contains a Walker A ATPase domain
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 276 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 10 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 309 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Peter T McKenney, Adam Driks, Patrick Eichenberger
The Bacillus subtilis endospore: assembly and functions of the multilayered coat.
Nat Rev Microbiol: 2013, 11(1);33-44
[PubMed:23202530] [WorldCat.org] [DOI] (I p)

Peter Setlow
Dynamics of the assembly of a complex macromolecular structure--the coat of spores of the bacterium Bacillus subtilis.
Mol Microbiol: 2012, 83(2);241-4
[PubMed:22192522] [WorldCat.org] [DOI] (I p)

Original publications