Response regulator aspartate phosphatases
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
Contents
The RAP proteins of B. subtilis, their cognate peptides and target proteins
- RapA, PhrA: RapA dephosphorylates Spo0F-P
- RapB: dephosphorylates Spo0F-P
- RapC, PhrC: RapC inhibits the DNA-binding activity of ComA-P
- RapD: RapD inhibits the DNA-binding activity of ComA-P
- RapE, PhrE: RapE dephosphorylates Spo0F-P
- RapF, PhrF: RapF inhibits the DNA-binding activity of ComA-P
- RapG, PhrG: RapG inhibits the DNA-binding activity of DegU-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
- RapJ: dephosphorylates Spo0F
- RapK, PhrK: RapK inhibits the DNA-binding activity of ComA-P
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Structural analysis
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Conformational change-induced repeat domain expansion regulates Rap phosphatase quorum-sensing signal receptors.
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Reviews
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Auxiliary phosphatases in two-component signal transduction.
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Daniel Schultz, Peter G Wolynes, Eshel Ben Jacob, José N Onuchic
Deciding fate in adverse times: sporulation and competence in Bacillus subtilis.
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M Perego, J A Brannigan
Pentapeptide regulation of aspartyl-phosphate phosphatases.
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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
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
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[PubMed:8730857]
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