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

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