Difference between revisions of "KinD"

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** 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 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}}
 
** 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}}
 +
** mainly active in the younger, outer regions of a colony (with [[KinC]]) {{PubMed|21097618}}
 +
 
* '''Protein family:'''
 
* '''Protein family:'''
  
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=References=
 
=References=
  
<pubmed>10094672,11069677,20689749 , </pubmed>
+
<pubmed>10094672,11069677,20689749 , 21097618 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:34, 29 November 2010

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
KinD context.gif
This image was kindly provided by SubtiList







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:
  • Localization:

Database entries

  • 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

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)