Difference between revisions of "KipA"

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m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
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* '''Operon:''' ''[[ycsF]]-[[ycsG]]-[[ycsI]]-[[kipI]]-[[kipA]]-[[kipR]]-[[lipC]]'' {{PubMed|9334321}}  
 
* '''Operon:''' ''[[ycsF]]-[[ycsG]]-[[ycsI]]-[[kipI]]-[[kipA]]-[[kipR]]-[[lipC]]'' {{PubMed|9334321}}  
  
* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=kipA_460592_461599_1 kipA] {{PubMed|22383849}}
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* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 14:30, 12 April 2012

Gene name kipA
Synonyms
Essential no
Product antagonist of KipI
Function control of the phosphorelay, initiation of sporulation
Interactions involving this protein in SubtInteract: KipA
Function and regulation of this protein in SubtiPathways:
Phosphorelay
MW, pI 36 kDa, 5.465
Gene length, protein length 1011 bp, 337 aa
Immediate neighbours kipI, kipR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
KipA context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

phosphorelay

This gene is a member of the following regulons

KipR regulon, TnrA regulon

The gene

Basic information

  • Locus tag: BSU04090

Phenotypes of a mutant

Database entries

  • 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:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • 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

David A Jacques, David B Langley, Robert M G Hynson, Andrew E Whitten, Ann Kwan, J Mitchell Guss, Jill Trewhella
A novel structure of an antikinase and its inhibitor.
J Mol Biol: 2011, 405(1);214-26
[PubMed:21050859] [WorldCat.org] [DOI] (I p)

L Wang, R Grau, M Perego, J A Hoch
A novel histidine kinase inhibitor regulating development in Bacillus subtilis.
Genes Dev: 1997, 11(19);2569-79
[PubMed:9334321] [WorldCat.org] [DOI] (P p)