DesK
Revision as of 10:25, 14 May 2013 by 134.76.70.252 (talk)
- Description: two-component sensor kinase, regulation of cold shock expression of des
Gene name | desK |
Synonyms | yocF |
Essential | no |
Product | two-component sensor kinase |
Function | regulation of cold shock expression of des |
Gene expression levels in SubtiExpress: desK | |
Interactions involving this protein in SubtInteract: DesK | |
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
MW, pI | 42 kDa, 9.428 |
Gene length, protein length | 1110 bp, 370 aa |
Immediate neighbours | des, desR |
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
lipid metabolism/ other, protein modification, transcription factors and their control, cold stress proteins, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU19190
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of DesR
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- 5 transmembrane helices
- cytoplasmatic C-terminal trail
- Modification: autophosphorylation on a His residue
- Cofactor(s):
- Effectors of protein activity: unsaturated fatty acids are negative effectors of the system
- Localization: membrane (transmembrane segments)
Database entries
- Structure: 3EHF
- UniProt: O34757
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- induced by cold shock (12-fold) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Diego de Mendoza, Universidad Nacional de Rosario, Argentine homepage
- Mohamed Marahiel, Marburg University, Germany homepage
Your additional remarks
References
Reviews
Richard C Stewart
Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.
Curr Opin Microbiol: 2010, 13(2);133-41
[PubMed:20117042]
[WorldCat.org]
[DOI]
(I p)
Pablo S Aguilar, Diego de Mendoza
Control of fatty acid desaturation: a mechanism conserved from bacteria to humans.
Mol Microbiol: 2006, 62(6);1507-14
[PubMed:17087771]
[WorldCat.org]
[DOI]
(P p)
Original publications