Difference between revisions of "KinC"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:01, 24 February 2015
- Description: two-component sensor kinase, phosphorylates Spo0F and Spo0A, part of the phosphorelay, governs expression of genes involved in biofilm formation
Gene name | kinC |
Synonyms | ssb |
Essential | no |
Product | two-component sensor kinase |
Function | initiation of sporulation |
Gene expression levels in SubtiExpress: kinC | |
Interactions involving this protein in SubtInteract: KinC | |
Function and regulation of this protein in SubtiPathways: kinC | |
MW, pI | 48 kDa, 6.225 |
Gene length, protein length | 1284 bp, 428 aa |
Immediate neighbours | abh, ykqA |
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
protein modification, transcription factors and their control, phosphorelay, biofilm formation, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14490
Phenotypes of a mutant
- defective in biofilm formation PubMed
Database entries
- BsubCyc: BSU14490
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- two transmembrane segments
- PAS domain
- C-terminal histidine phosphotransferase domain
- Modification: autophosphorylation on a His residue
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU14490
- Structure:
- UniProt: P39764
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: kinC (according to DBTBS)
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications