Difference between revisions of "SpoIVA"
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' contains a Walker A ATPase domain |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spoIVA_2386195_2387673_-1 spoIVA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spoIVA_2386195_2387673_-1 spoIVA] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigE]] {{PubMed|1729246,15699190}} | + | * '''[[Sigma factor]]:''' [[SigE]] {{PubMed|1729246,15699190}} |
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 18:12, 4 January 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
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:
- Localization:
- spore coat (basement) PubMed
Database entries
- Structure:
- UniProt: P35149
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: spoIVA PubMed
- Additional information:
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