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
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU14490

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

• 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

• Interactions: KinC-Spo0A PubMed, KinC-Spo0F

• Localization: cell membrane (Heterogeneous) PubMed

Database entries

• Structure:

• UniProt: P39764

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: kinC (according to DBTBS)

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)