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

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

Related lists

Structural analysis

Reviews