SpoIVA

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

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

• CotE, LipC, SpoVM, SpoVID, YhaX, YheD, YjzB, YppG PubMed

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

• BsubCyc: BSU22800

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • SpoIVA-SpoVID PubMed
  • SpoIVA-SafA PubMed
  • SpoIVA-SpoVM-SpoVID PubMed

• Localization:
  • innermost protein of the spore coat basement PubMed

Database entries

• BsubCyc: BSU22800

• Structure:

• UniProt: P35149

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: spoIVA PubMed

• Expression browser: spoIVA PubMed

• Sigma factor: SigE PubMed

• Regulation:
  • expressed early during sporulation in the mother cell (SigE, SpoIIID) PubMed

• Regulatory mechanism:
  • SpoIIID: transcription repression PubMed

• 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:

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)