KinC

• Description: 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
  
  

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: Phosphorelay
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

• 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

• 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 triggered by potassium leakage 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

Database entries

• 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

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)