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 |
Contents
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
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]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 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:
Database entries
- BsubCyc: BSU14490
- Structure:
- UniProt: P39764
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: kinC (according to DBTBS)
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)