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Literature summary for 2.7.13.3 extracted from

  • Devi, S.N.; Vishnoi, M.; Kiehler, B.; Haggett, L.; Fujita, M.
    In vivo functional characterization of the transmembrane histidine kinase KinC in Bacillus subtilis (2015), Microbiology, 161, 1092-1104.
    View publication on PubMed
Search for more literature for 2.7.13.3

Activating Compound

Activating Compound Comment Organism Structure
additional information KinC becomes active by forming a homotetramer via the N-terminal PAS domain, but its activity is independent of both the lipid raft and the potassium leakage Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme KinC in Escherichia coli strain BL21(DE3) Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information in vivo quantitative domain-based stepwise deletion analyses to determine the minimum functional domain of KinC, overview Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell membrane KinC localizes as puncta along the cell membrane in a manner independent of FloTA proteins, localization pattern of GFP-tagged KinC, overview. KinC does not localize at specific sites on membrane under the conditions tested Bacillus subtilis
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Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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 competent NCIB 3610 strains PY79 and DK1042 comIQ12L
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Bacillus subtilis 168
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 competent NCIB 3610 strains PY79 and DK1042 comIQ12L
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme KinC from Escherichia coli strain BL21(DE3) by nicke affinity chromatography Bacillus subtilis

Subunits

Subunits Comment Organism
homotetramer KinC becomes active by forming a homotetramer via the N-terminal PAS domain Bacillus subtilis
More the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity Bacillus subtilis

Synonyms

Synonyms Comment Organism
KinC
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 Bacillus subtilis
sporulation kinase
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 Bacillus subtilis

General Information

General Information Comment Organism
metabolism in response to starvation, Bacillus subtilis cells differentiate into different subsets, undergoing cannibalism, biofilm formation or sporulation. These processes require a multiple component phosphorelay, wherein the master regulator Spo0A is activated upon phosphorylation by one or a combination of five histidine kinases (KinA-KinE) via two intermediate phosphotransferases, Spo0F and Spo0B. KinC controls the expression of cannibalism genes in a manner independent of surfactin andthe bacterial flotillin-like proteins FloT and FloA Bacillus subtilis
additional information the N-terminal transmembrane domain is dispensable but the PAS domain is needed for the kinase activity Bacillus subtilis
physiological function enzyme KinC regulates cannibalism and biofilm formation, and activates the expression of cannibalism genes in response to starvation in a manner dependent on phosphorelay. KinC activity and the membrane localization are independent of both the lipid raft marker proteins FloTA and cytoplasmic potassium concentration. KinC becomes active by forming a homotetramer via the N-terminal PAS domain Bacillus subtilis