Phosphoproteins

These proteins are subject to a phosphorylation event. Most often, protein phosphorylation affects the conformation of the protein resulting in changes in biological activity and/ or localization.

Phosphoproteins in B. subtilis

Phosphorylation on an Arg residue

• CtsR, phosphorylated by McsB

Phosphorylation on a His residue=

• PTS proteins
  • Enzyme I: autophosphorylated using phosphoenolpyruvate as phosphate donor
  • HPr: phosphorylated by Enzyme I
  • PtsG: glucose permease, EIICBA: phosphorylated by HPr
  • GamP: glucosamine permease, EIICBA: phosphorylated by HPr
  • MtlA, MtlF: mannitol permease: phosphorylated by HPr
  • GmuA, GmuB, GmuC: galactomannan permease: phosphorylated by HPr
  • TreP: trehalose permease: phosphorylated by HPr
  • MalP: maltose permease: phosphorylated by HPr
  • FruA: fructose permease: phosphorylated by HPr
  • ManP: mannose permease: phosphorylated by HPr
  • LevD, LevE, LevF, LevG: fructose permease: phosphorylated by HPr
  • LicA, LicB, LicC: lichenan permease: phosphorylated by HPr
  • BglP: ß-glucoside permease
  • YpqE: unknown EIIA component: phosphorylated by HPr
  • YyzE: unknown PTS protein

• Non-PTS proteins controlled by PTS-dependent phosphorylation
  • GlpK: phosphorylated by HPr
  • GlcT: phosphorylated by HPr and by PtsG
  • LicT: phosphorylated by HPr and likely by BglP
  • SacT: phosphorylated by HPr and likely by SacP
  • SacY: phosphorylated by HPr and likely by SacY
  • LevR: phosphorylated by HPr and by LevE
  • LicR: phosphorylated by HPr and likely by LicB
  • ManR: phosphorylated by HPr and likely by ManP
  • MtlR: phosphorylated by HPr and likely by MtlA

Proteins closely related to the PTS

• Crh: HPr-like protein with exculsively regulatory functions (His-15 is not conserved
• HprK: HPr-kinase, key factor for carbon catabolite repression

Related Lists

• two-component systems
• PTS
• PRD-containing transcription factors
• phosphorelay
• response regulator aspartate phosphatases

Original papers on the B. subtilis phosphoproteome

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)