Difference between revisions of "DynA"
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+ | <pubmed> 23109540 20970992 21599493 15040446 </pubmed> | ||
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<pubmed> 8396117 21205012 20525796 23060960</pubmed> | <pubmed> 8396117 21205012 20525796 23060960</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:02, 23 November 2012
- Description: dynamin-like protein, mediates membrane fusion
Gene name | dynA |
Synonyms | ypbR |
Essential | no |
Product | dynamin-like protein |
Function | fusion of membranes |
Gene expression levels in SubtiExpress: dynA | |
Interactions involving this protein in SubtInteract: DynA | |
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
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
membrane dynamics, membrane proteins
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:
Database entries
- Structure:
- UniProt: P54159
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: dynA PubMed
- Regulation:
- Regulatory mechanism:
- 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
Marc Bramkamp
Structure and function of bacterial dynamin-like proteins.
Biol Chem: 2012, 393(11);1203-14
[PubMed:23109540]
[WorldCat.org]
[DOI]
(I p)
Sandra L Schmid, Vadim A Frolov
Dynamin: functional design of a membrane fission catalyst.
Annu Rev Cell Dev Biol: 2011, 27;79-105
[PubMed:21599493]
[WorldCat.org]
[DOI]
(I p)
Harry H Low, Jan Löwe
Dynamin architecture--from monomer to polymer.
Curr Opin Struct Biol: 2010, 20(6);791-8
[PubMed:20970992]
[WorldCat.org]
[DOI]
(I p)
Gerrit J K Praefcke, Harvey T McMahon
The dynamin superfamily: universal membrane tubulation and fission molecules?
Nat Rev Mol Cell Biol: 2004, 5(2);133-47
[PubMed:15040446]
[WorldCat.org]
[DOI]
(P p)
Original publications