Difference between revisions of "KinD"
(→Basic information/ Evolution) |
|||
| Line 1: | Line 1: | ||
| − | * '''Description:''' [[two-component systems|two-component]] sensor kinase, phosphorylates [[Spo0F]], part of the [[phosphorelay]], checkpoint protein that links sporulation initiation to the formation of the biofilm matrix <br/><br/> | + | * '''Description:''' [[two-component systems|two-component]] sensor [[protein kinases and phosphatases|kinase]], phosphorylates [[Spo0F]], part of the [[phosphorelay]], checkpoint protein that links sporulation initiation to the formation of the biofilm matrix <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 56: | Line 56: | ||
* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
** autophosphorylation, phosphorylation of [[Spo0F]], regulates the onset of sporulation by inhibiting the activity of [[Spo0A]] until matrix, or a component therein, is sensed [http://mbio.asm.org/content/1/1/e00035-10.full PubMed] | ** autophosphorylation, phosphorylation of [[Spo0F]], regulates the onset of sporulation by inhibiting the activity of [[Spo0A]] until matrix, or a component therein, is sensed [http://mbio.asm.org/content/1/1/e00035-10.full PubMed] | ||
| − | ** dual role as a [[protein phosphatase]] or a [[protein kinase]], activity is linked to the presence of extracellular matrix in the biofilms {{PubMed|20689749}} | + | ** dual role as a [[protein kinases and phosphatases|phosphatase]] or a [[protein kinases and phosphatases|kinase]], activity is linked to the presence of extracellular matrix in the biofilms {{PubMed|20689749}} |
* '''Protein family:''' | * '''Protein family:''' | ||
Revision as of 10:58, 7 August 2010
- Description: two-component sensor kinase, phosphorylates Spo0F, part of the phosphorelay, checkpoint protein that links sporulation initiation to the formation of the biofilm matrix
| Gene name | kinD |
| Synonyms | ykvD |
| Essential | no |
| Product | two-component sensor kinase |
| Function | initiation of sporulation |
| Function and regulation of this protein in SubtiPathways: Phosphorelay | |
| MW, pI | 56 kDa, 6.745 |
| Gene length, protein length | 1518 bp, 506 aa |
| Immediate neighbours | eag, mhqR |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU13660
Phenotypes of a mutant
deletion of kinD suppresses the sporulation defect of matrix mutants, while its overproduction delays sporulation PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
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, C-terminal histidine phosphotransferase domain
- Modification: autophosphorylation on a His residue
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure: 3FOS
- UniProt: O31671
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
Claudio Aguilar, Hera Vlamakis, Alejandra Guzman, Richard Losick, Roberto Kolter
KinD is a checkpoint protein linking spore formation to extracellular-matrix production in Bacillus subtilis biofilms.
mBio: 2010, 1(1);
[PubMed:20689749]
[WorldCat.org]
[DOI]
(I e)
M Jiang, W Shao, M Perego, J A Hoch
Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis.
Mol Microbiol: 2000, 38(3);535-42
[PubMed:11069677]
[WorldCat.org]
[DOI]
(P p)
C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672]
[WorldCat.org]
[DOI]
(P p)
