Difference between revisions of "ResE"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:35, 16 October 2012
- Description: two-component sensor kinase, regulation of aerobic and anaerobic respiration
Gene name | resE |
Synonyms | ypxE |
Essential | no |
Product | two-component sensor kinase |
Function | regulation of aerobic and anaerobic respiration |
Gene expression levels in SubtiExpress: resE | |
Interactions involving this protein in SubtInteract: ResE | |
MW, pI | 66 kDa, 5.344 |
Gene length, protein length | 1767 bp, 589 aa |
Immediate neighbours | sigX, resD |
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
regulators of electron transport, protein modification, transcription factors and their control, membrane proteins, phosphoproteins
This gene is a member of the following regulons
CcpA regulon, PhoP regulon, ResD regulon
The gene
Basic information
- Locus tag: BSU23110
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 ResD
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains: two transmembrane segments, C-terminal histidine phosphotransferase domain
- Modification: autophosphorylation on a His residue
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P35164
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Original publications