Difference between revisions of "DynA"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''Interactions:''' forms oligomers {{PubMed|21205012}} |
| − | * '''Localization:''' | + | * '''Localization:''' associated to the membrane {{PubMed|21205012}} |
=== Database entries === | === Database entries === | ||
Revision as of 13:31, 6 January 2011
- Description: dynamin-like protein, mediates membrane fusion
| Gene name | dynA |
| Synonyms | ypbR |
| Essential | no |
| Product | dynamin-like protein |
| Function | fusion of membranes |
| MW, pI | 137 kDa, 5.724 |
| Gene length, protein length | 3579 bp, 1193 aa |
| Immediate neighbours | ypbS, fbpC |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU22030
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: mediates nucleotide independent membrane fusion in vitro PubMed
- Protein family: gerABKA family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains: two separate dynamin-like subunits and GTPase domains PubMed
- Modification:
- Cofactor(s): Mg(2+) PubMed
- Effectors of protein activity:
- Interactions: forms oligomers PubMed
- Localization: associated to the membrane PubMed
Database entries
- Structure:
- UniProt: P54159
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: ypbR 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
Frank Bürmann, Nina Ebert, Suey van Baarle, Marc Bramkamp
A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion.
Mol Microbiol: 2011, 79(5);1294-304
[PubMed:21205012]
[WorldCat.org]
[DOI]
(I p)
L Chen, L P James, J D Helmann
Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions.
J Bacteriol: 1993, 175(17);5428-37
[PubMed:8396117]
[WorldCat.org]
[DOI]
(P p)
