Difference between revisions of "KinD"
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
+ | ** activity is stimulated by direct or indirect [[interaction]] with [[Med]] {{PubMed|21622736}} | ||
* '''Interactions:''' [[KinD]]-[[Spo0F]] | * '''Interactions:''' [[KinD]]-[[Spo0F]] | ||
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=References= | =References= | ||
− | + | '''Additonal publications:''' {{PubMed|21622736}} | |
<pubmed>10094672,11069677,20689749 , 21097618 </pubmed> | <pubmed>10094672,11069677,20689749 , 21097618 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:47, 10 June 2011
- Description: two-component sensor kinase, phosphorylates Spo0F, part of the phosphorelay, checkpoint protein that links sporulation initiation to biofilm formation
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
Categories containing this gene/protein
protein modification, transcription factors and their control, phosphorelay, membrane proteins, phosphoproteins
This gene is a member of the following regulons
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:
- autophosphorylation, phosphorylation of Spo0F, regulates the onset of sporulation by inhibiting the activity of Spo0A until matrix, or a component therein, is sensed PubMed
- dual role as a phosphatase or a kinase, activity is linked to the presence of extracellular matrix in the biofilms PubMed
- mainly active in the younger, outer regions of a colony (with KinC) PubMed
- 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:
- activity is stimulated by direct or indirect interaction with Med PubMed
- 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
Additonal publications: PubMed
Anna L McLoon, Ilana Kolodkin-Gal, Shmuel M Rubinstein, Roberto Kolter, Richard Losick
Spatial regulation of histidine kinases governing biofilm formation in Bacillus subtilis.
J Bacteriol: 2011, 193(3);679-85
[PubMed:21097618]
[WorldCat.org]
[DOI]
(I p)
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)