Difference between revisions of "KinD"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=KinD KinD]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=KinD KinD]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/phosphorelay.html Phosphorelay]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=kinD kinD]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 56 kDa, 6.745   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 56 kDa, 6.745   

Revision as of 10:37, 7 January 2014

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
KinD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
KinD expression.png















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: BSU13660

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

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

Database entries

  • Structure: 4DBJ (extracytoplasmic sensing domain) PubMed
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

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)