KinD

• Description: two-component sensor kinase, phosphorylates Spo0F, part of the phosphorelay, checkpoint protein that links sporulation initiation to biofilm formation
  
  

Gene name	kinD
Synonyms	ykvD
Essential	no
Product	two-component sensor kinase
Function	initiation of sporulation
Gene expression levels in SubtiExpress: kinD
Interactions involving this protein in SubtInteract: KinD
Function and regulation of this protein in SubtiPathways: Phosphorelay
MW, pI	56 kDa, 6.745
Gene length, protein length	1518 bp, 506 aa
Immediate neighbours	eag, mhqR
Get the DNA and protein sequences (Barbe et al., 2009)
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

The gene

Basic information

• Locus tag: BSU13660

Phenotypes of a mutant

• deletion of kinD suppresses the sporulation defect of matrix mutants, while its overproduction delays sporulation PubMed
• inactivation of kinD restores beta-lactam resistance in a sigM mutant PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • autophosphorylation, phosphorylation of Spo0F, regulates the onset of sporulation by inhibiting the activity of Spo0A until matrix, or a component therein, is sensed PubMed
  • dual role as a phosphatase or a kinase, activity is linked to the presence of extracellular matrix in the biofilms PubMed
  • mainly active in the younger, outer regions of a colony (with KinC) PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • two transmembrane segments, between them the extracellular CACHE domain for L-malate binding PubMed
  • C-terminal histidine phosphotransferase domain
  • see PubMed for a scheme of the domain organization

• Modification: autophosphorylation on a His residue

• Cofactor(s):

• Effectors of protein activity:
  • activity is stimulated by direct or indirect interaction with Med PubMed
  • L-malate seems to trigger KinD activity PubMed

• Interactions:
  • KinD-Spo0F

• Localization: membrane

Database entries

• Structure: 3FOS

• UniProt: O31671

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: kinD PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additonal publications: PubMed

Yun Chen, Shugeng Cao, Yunrong Chai, Jon Clardy, Roberto Kolter, Jian-hua Guo, Richard Losick
A Bacillus subtilis sensor kinase involved in triggering biofilm formation on the roots of tomato plants.
Mol Microbiol: 2012, 85(3);418-30
[PubMed:22716461] [WorldCat.org] [DOI] (I p)

Elizabeth A Shank, Vanja Klepac-Ceraj, Leonardo Collado-Torres, Gordon E Powers, Richard Losick, Roberto Kolter
Interspecies interactions that result in Bacillus subtilis forming biofilms are mediated mainly by members of its own genus.
Proc Natl Acad Sci U S A: 2011, 108(48);E1236-43
[PubMed:22074846] [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)

Claudio Aguilar, Hera Vlamakis, Alejandra Guzman, Richard Losick, Roberto Kolter
KinD is a checkpoint protein linking spore formation to extracellular-matrix production in Bacillus subtilis biofilms.
mBio: 2010, 1(1);
[PubMed:20689749] [WorldCat.org] [DOI] (I e)

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)