KinD

• Description: osmo-sensing 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: kinD
MW, pI	56 kDa, 6.745
Gene length, protein length	1518 bp, 506 aa
Immediate neighbours	eag, mhqR
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

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

• BsubCyc: BSU13660

• 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 pyruvate-binding sensing domain that consists of tandem PAS-like domains 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, but this effect may be indirect due to the excretion of pyruvate that directly binds the extracytoplasmic sensing domain of KinD PubMed
  • kinase activity is triggered and phosphatase activity is decreased by increased osmotic pressure PubMed
  • activity is triggered in the presence of glycerol + manganese PubMed

• Interactions:
  • KinD-Spo0F

• Localization: membrane

Database entries

• BsubCyc: BSU13660

• Structure: 4DBJ (extracytoplasmic sensing domain) PubMed

• 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

Moshe Shemesh, Yunrong Chai
A combination of glycerol and manganese promotes biofilm formation in Bacillus subtilis via histidine kinase KinD signaling.
J Bacteriol: 2013, 195(12);2747-54
[PubMed:23564171] [WorldCat.org] [DOI] (I p)

R Wu, M Gu, R Wilton, G Babnigg, Y Kim, P R Pokkuluri, H Szurmant, A Joachimiak, M Schiffer
Insight into the sporulation phosphorelay: crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD.
Protein Sci: 2013, 22(5);564-76
[PubMed:23436677] [WorldCat.org] [DOI] (I p)

Shmuel M Rubinstein, Ilana Kolodkin-Gal, Anna McLoon, Liraz Chai, Roberto Kolter, Richard Losick, David A Weitz
Osmotic pressure can regulate matrix gene expression in Bacillus subtilis.
Mol Microbiol: 2012, 86(2);426-36
[PubMed:22882172] [WorldCat.org] [DOI] (I p)

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)

Yun Luo, John D Helmann
Analysis of the role of Bacillus subtilis σ(M) in β-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis.
Mol Microbiol: 2012, 83(3);623-39
[PubMed:22211522] [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)

Allison V Banse, Errett C Hobbs, Richard Losick
Phosphorylation of Spo0A by the histidine kinase KinD requires the lipoprotein med in Bacillus subtilis.
J Bacteriol: 2011, 193(15);3949-55
[PubMed:21622736] [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)