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). 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

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Structural analysis

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Ruth E Silversmith
Auxiliary phosphatases in two-component signal transduction.
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Daniel Schultz, Peter G Wolynes, Eshel Ben Jacob, José N Onuchic
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M Perego, J A Brannigan
Pentapeptide regulation of aspartyl-phosphate phosphatases.
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[PubMed:11587783] [] [DOI] (P p)

J Reizer, A Reizer, M Perego, M H Saier
Characterization of a family of bacterial response regulator aspartyl-phosphate (RAP) phosphatases.
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M Perego, P Glaser, J A Hoch
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