KinC

• Description: two-component sensor kinase, phosphorylates Spo0F and Spo0A, part of the phosphorelay, governs expression of genes involved in biofilm formation
  
  

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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• • defective in biofilm formation PubMed

Database entries

• BsubCyc: BSU14490

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Interactions:
  • KinC-Spo0A PubMed
  • KinC-Spo0F

• Localization:
  • cell membrane (Heterogeneous) PubMed
  • co-localizes with FloT in discrete foci in the membrane PubMed
  • the localization of KinC in membrane microdomains depends on FloA and FloT PubMed, this has been refuted PubMed

Database entries

• BsubCyc: BSU14490

• Structure:

• UniProt: P39764

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: kinC (according to DBTBS)

• Expression browser: kinC PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:
  • 1A632 ( kinC::erm), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Daniel López
Connection of KinC to flotillins and potassium leakage in Bacillus subtilis.
Microbiology (Reading): 2015, 161(6);1180-1
[PubMed:25934647] [WorldCat.org] [DOI] (I p)

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

Roberto R Grau, Paula de Oña, Maritta Kunert, Cecilia Leñini, Ramses Gallegos-Monterrosa, Eisha Mhatre, Darío Vileta, Verónica Donato, Theresa Hölscher, Wilhelm Boland, Oscar P Kuipers, Ákos T Kovács
A Duo of Potassium-Responsive Histidine Kinases Govern the Multicellular Destiny of Bacillus subtilis.
mBio: 2015, 6(4);e00581
[PubMed:26152584] [WorldCat.org] [DOI] (I e)

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)