Difference between revisions of "Response regulator aspartate phosphatases"

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These proteins contain the so-called tetratricopeptide repeats (TPRs) protein-protein interaction module. They control the [[phosphorelay]] for sporulation initiation by dephosphorylating [[Spo0F]]-P or they inhibit transcription factors by protein-protein interaction (without affecting phosphorylation).
 
These proteins contain the so-called tetratricopeptide repeats (TPRs) protein-protein interaction module. They control the [[phosphorelay]] for sporulation initiation by dephosphorylating [[Spo0F]]-P or they inhibit transcription factors by protein-protein interaction (without affecting phosphorylation).
 
The activity of these proteins can be controlled by small peptides that are expressed as precursors, exported, and re-imported into the cell.
 
The activity of these proteins can be controlled by small peptides that are expressed as precursors, exported, and re-imported into the cell.
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The RAP phosphatases are made up of the C-terminal tetratricopeptide repeat (TPR) domain that is connected by a flexible helix containing linker to the N-terminal 3-helix bundle. Upon binding of the regulating peptide, the 3-helix bundle and the linker helix undergo a conformational change to form a TPR-like fold that merges with the existing C-terminal TPR domain. {{PubMed|23526881}}
  
 
==The RAP proteins of ''B. subtilis'', their cognate peptides and target proteins==
 
==The RAP proteins of ''B. subtilis'', their cognate peptides and target proteins==
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* [[RapH]]: bifuntional protein: dephosphorylates [[Spo0F]]-P and inhibits the DNA-binding activity of [[ComA]]-P
 
* [[RapH]]: bifuntional protein: dephosphorylates [[Spo0F]]-P and inhibits the DNA-binding activity of [[ComA]]-P
 
* [[RapI]], [[PhrI]]: [[RapI]] inhibits the DNA-binding activity of [[ImmR]]
 
* [[RapI]], [[PhrI]]: [[RapI]] inhibits the DNA-binding activity of [[ImmR]]
* [[RapJ]]: unknown function
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* [[RapJ]]: dephosphorylates [[Spo0F]]
 
* [[RapK]], [[PhrK]]: [[RapK]] inhibits the DNA-binding activity of [[ComA]]-P
 
* [[RapK]], [[PhrK]]: [[RapK]] inhibits the DNA-binding activity of [[ComA]]-P
  
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* [[two-component systems]]
 
* [[two-component systems]]
 
* [[phosphorelay]]
 
* [[phosphorelay]]
 
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* [[phosphoproteins]]
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* [[protein kinases and phosphatases]]
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==Structural analysis==
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<pubmed> 23526881 </pubmed>
 
==Reviews==
 
==Reviews==
<pubmed>8730857 11587783 19995980 </pubmed>
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<pubmed>8730857 11587783 19995980 9689219 20133180 </pubmed>

Latest revision as of 17:36, 27 March 2013

These proteins contain the so-called tetratricopeptide repeats (TPRs) protein-protein interaction module. They control the phosphorelay for sporulation initiation by dephosphorylating Spo0F-P or they inhibit transcription factors by protein-protein interaction (without affecting phosphorylation). The activity of these proteins can be controlled by small peptides that are expressed as precursors, exported, and re-imported into the cell.

The RAP phosphatases are made up of the C-terminal tetratricopeptide repeat (TPR) domain that is connected by a flexible helix containing linker to the N-terminal 3-helix bundle. Upon binding of the regulating peptide, the 3-helix bundle and the linker helix undergo a conformational change to form a TPR-like fold that merges with the existing C-terminal TPR domain. PubMed

The RAP proteins of B. subtilis, their cognate peptides and target proteins

Related lists

Structural analysis

Reviews