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/>
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* '''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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= [[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}}  
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** 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:'''  
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** activity is triggered by potassium leakage {{PubMed|19114652}}
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** 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}}
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** 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 ==
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<pubmed>19114652,10094672,11069677,16166384, 20713508,8002615, 16479537 8002614 20946851 20971918 21097618 22882210 23927765 </pubmed>
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<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

Marc Bramkamp, Daniel Lopez
Exploring the existence of lipid rafts in bacteria.
Microbiol Mol Biol Rev: 2015, 79(1);81-100
[PubMed:25652542] [WorldCat.org] [DOI] (I p)

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)

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