Difference between revisions of "KinC"

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* '''Description:''' [[two-component systems|two-component]] sensor kinase, phosphorylates [[Spo0F]] and [[Spo0A]] in response to the presence of surfactin, part of the [[phosphorelay]], governs expression of genes involved in [[biofilm formation]] <br/><br/>
+
* '''Description:''' [[two-component systems|two-component]] sensor kinase, phosphorylates [[Spo0F]] and [[Spo0A]], part of the [[phosphorelay]], governs expression of genes involved in [[biofilm formation]] <br/><br/>
  
 
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{| align="right" border="1" cellpadding="2"  
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<br/><br/><br/><br/>
 
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<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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** autophosphorylation, phosphorylation of [[Spo0F]] as part of the [[phosphorelay]], but also direct phosphorylation of [[Spo0A]] {{PubMed|19114652}}
 
** autophosphorylation, phosphorylation of [[Spo0F]] as part of the [[phosphorelay]], but also direct phosphorylation of [[Spo0A]] {{PubMed|19114652}}
 
** mainly active in the younger, outer regions of a colony (with [[KinD]]) {{PubMed|21097618}}  
 
** mainly active in the younger, outer regions of a colony (with [[KinD]]) {{PubMed|21097618}}  
** phosphorylates [[Spo0A]] in response to the presence of surfactin {{PubMed|22882210}}  
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** phosphorylates [[Spo0A]] in response to the presence of surfactin {{PubMed|22882210}}, this has been refuted {{PubMed|25701730}}
  
 
* '''Protein family:'''
 
* '''Protein family:'''
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* '''Effectors of protein activity:'''  
 
* '''Effectors of protein activity:'''  
** activity is triggered by potassium leakage {{PubMed|19114652}}
+
** activity is triggered by potassium leakage {{PubMed|19114652}}, this has been refuted {{PubMed|25701730}}
 
** activity is triggered by polyisoprenoid lipids formed by [[YisP]] {{PubMed|20713508}}
 
** activity is triggered by polyisoprenoid lipids formed by [[YisP]] {{PubMed|20713508}}
 
   
 
   
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** cell membrane (Heterogeneous) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
 
** cell membrane (Heterogeneous) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
 
** co-localizes with [[FloT]] in discrete foci in the membrane {{PubMed|20713508}}
 
** co-localizes with [[FloT]] in discrete foci in the membrane {{PubMed|20713508}}
** the localization of [[KinC]] in membrane microdomains depends on [[FloA]] and [[FloT]]  {{PubMed|22882210}}
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** the localization of [[KinC]] in membrane microdomains depends on [[FloA]] and [[FloT]]  {{PubMed|22882210}}, this has been refuted {{PubMed|25701730}}
  
 
=== Database entries ===
 
=== Database entries ===
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<pubmed> 25652542</pubmed>
 
<pubmed> 25652542</pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed>19114652,10094672,11069677,16166384, 20713508,8002615, 16479537 8002614 20946851 20971918 21097618 22882210 23927765 </pubmed>
+
<pubmed>19114652,10094672,11069677,16166384, 20713508,8002615, 16479537 8002614 20946851 20971918 21097618 22882210 23927765 25701730</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:02, 23 February 2015

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
KinC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
KinC expression.png















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

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU14490

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 Spo0F as part of the phosphorelay, but also direct phosphorylation of Spo0A PubMed
    • mainly active in the younger, outer regions of a colony (with KinD) PubMed
    • phosphorylates Spo0A in response to the presence of surfactin PubMed, this has been refuted PubMed
  • 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:
    • activity is triggered by potassium leakage PubMed, this has been refuted PubMed
    • activity is triggered by polyisoprenoid lipids formed by YisP PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: kinC (according to DBTBS)
  • Regulation:
    • expressed under conditions that trigger sporulation (Spo0A) PubMed
  • 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

Seram Nganbiton Devi, Monika Vishnoi, Brittany Kiehler, Lindsey Haggett, Masaya Fujita
In vivo functional characterization of the transmembrane histidine kinase KinC in Bacillus subtilis.
Microbiology (Reading): 2015, 161(Pt 5);1092-1104
[PubMed:25701730] [WorldCat.org] [DOI] (I p)

Monika Vishnoi, Jatin Narula, Seram Nganbiton Devi, Hoang-Anh Dao, Oleg A Igoshin, Masaya Fujita
Triggering sporulation in Bacillus subtilis with artificial two-component systems reveals the importance of proper Spo0A activation dynamics.
Mol Microbiol: 2013, 90(1);181-94
[PubMed:23927765] [WorldCat.org] [DOI] (I p)

Ana Yepes, Johannes Schneider, Benjamin Mielich, Gudrun Koch, Juan-Carlos García-Betancur, Kumaran S Ramamurthi, Hera Vlamakis, Daniel López
The biofilm formation defect of a Bacillus subtilis flotillin-defective mutant involves the protease FtsH.
Mol Microbiol: 2012, 86(2);457-71
[PubMed:22882210] [WorldCat.org] [DOI] (I p)

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)

Moshe Shemesh, Roberto Kolter, Richard Losick
The biocide chlorine dioxide stimulates biofilm formation in Bacillus subtilis by activation of the histidine kinase KinC.
J Bacteriol: 2010, 192(24);6352-6
[PubMed:20971918] [WorldCat.org] [DOI] (I p)

Daniel López, Erin A Gontang, Roberto Kolter
Potassium sensing histidine kinase in Bacillus subtilis.
Methods Enzymol: 2010, 471;229-51
[PubMed:20946851] [WorldCat.org] [DOI] (I p)

Daniel López, Roberto Kolter
Functional microdomains in bacterial membranes.
Genes Dev: 2010, 24(17);1893-902
[PubMed:20713508] [WorldCat.org] [DOI] (I p)

Daniel López, Michael A Fischbach, Frances Chu, Richard Losick, Roberto Kolter
Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2009, 106(1);280-5
[PubMed:19114652] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Masaya Fujita, Richard Losick
Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A.
Genes Dev: 2005, 19(18);2236-44
[PubMed:16166384] [WorldCat.org] [DOI] (P p)

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)

K Kobayashi, K Shoji, T Shimizu, K Nakano, T Sato, Y Kobayashi
Analysis of a suppressor mutation ssb (kinC) of sur0B20 (spo0A) mutation in Bacillus subtilis reveals that kinC encodes a histidine protein kinase.
J Bacteriol: 1995, 177(1);176-82
[PubMed:8002615] [WorldCat.org] [DOI] (P p)

J R LeDeaux, A D Grossman
Isolation and characterization of kinC, a gene that encodes a sensor kinase homologous to the sporulation sensor kinases KinA and KinB in Bacillus subtilis.
J Bacteriol: 1995, 177(1);166-75
[PubMed:8002614] [WorldCat.org] [DOI] (P p)