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

• two-component systems
• phosphorelay
• phosphoproteins
• protein kinases and phosphatases

Structural analysis

Vijay Parashar, Philip D Jeffrey, Matthew B Neiditch
Conformational change-induced repeat domain expansion regulates Rap phosphatase quorum-sensing signal receptors.
PLoS Biol: 2013, 11(3);e1001512
[PubMed:23526881] [WorldCat.org] [DOI] (I p)

Reviews

Ruth E Silversmith
Auxiliary phosphatases in two-component signal transduction.
Curr Opin Microbiol: 2010, 13(2);177-83
[PubMed:20133180] [WorldCat.org] [DOI] (I p)

Daniel Schultz, Peter G Wolynes, Eshel Ben Jacob, José N Onuchic
Deciding fate in adverse times: sporulation and competence in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2009, 106(50);21027-34
[PubMed:19995980] [WorldCat.org] [DOI] (I p)

M Perego, J A Brannigan
Pentapeptide regulation of aspartyl-phosphate phosphatases.
Peptides: 2001, 22(10);1541-7
[PubMed:11587783] [WorldCat.org] [DOI] (P p)

J Reizer, A Reizer, M Perego, M H Saier
Characterization of a family of bacterial response regulator aspartyl-phosphate (RAP) phosphatases.
Microb Comp Genomics: 1997, 2(2);103-11
[PubMed:9689219] [WorldCat.org] [DOI] (P p)

M Perego, P Glaser, J A Hoch
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
Mol Microbiol: 1996, 19(6);1151-7
[PubMed:8730857] [WorldCat.org] [DOI] (P p)