Difference between revisions of "KinD"

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* '''Domains:'''  
 
* '''Domains:'''  
** two transmembrane segments, between them the extracellular CACHE domain for L-malate binding {{PubMed|22716461}}
+
** two transmembrane segments, between them the extracellular pyruvate-binding sensing domain that consists of tandem PAS-like domains {{PubMed|23436677,22716461}}
 
** C-terminal histidine phosphotransferase domain
 
** C-terminal histidine phosphotransferase domain
 
** see {{PubMed|22716461}} for a scheme of the domain organization
 
** see {{PubMed|22716461}} for a scheme of the domain organization
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
 
** activity is stimulated by direct or indirect interaction with [[Med]] {{PubMed|21622736}}
 
** activity is stimulated by direct or indirect interaction with [[Med]] {{PubMed|21622736}}
** L-malate seems to trigger KinD activity {{PubMed|22716461}}
+
** L-malate seems to trigger KinD activity {{PubMed|22716461}}, but this effect may be indirect due to the excretion of pyruvate that directly binds the extracytoplasmic sensing domain of KinD {{PubMed|23436677}}
 
** kinase activity is triggered and phosphatase activity is decreased by increased osmotic pressure {{PubMed|22882172}}
 
** kinase activity is triggered and phosphatase activity is decreased by increased osmotic pressure {{PubMed|22882172}}
  
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3FOS 3FOS]
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=4DBJ 4DBJ] (extracytoplasmic sensing domain) {{PubMed|23436677}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31671 O31671]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31671 O31671]
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=References=
 
=References=
 
'''Additonal publications:''' {{PubMed|21622736,22211522}}
 
'''Additonal publications:''' {{PubMed|21622736,22211522}}
<pubmed>10094672,11069677,20689749 , 21097618  22074846 22716461 22882172 </pubmed>
+
<pubmed>10094672,11069677,20689749 , 21097618  22074846 22716461 22882172 23436677 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:11, 26 February 2013

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
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

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

Additonal publications: PubMed

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)

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)