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 an Asp residue: Response regulators of two-component systems

• ComA: phosphorylated by ComP
• DegU: phosphorylated by DegS
• DesR: phosphorylated by DesK
• LiaR: phosphorylated by LiaS
• YdfI: phosphorylated by YdfH
• YfiK: phosphorylated by YfiJ
• YhcZ: phosphorylated by YhcY
• YvfU: phosphorylated by YvfT
• YxjL: phosphorylated by YxjM
• BceR: phosphorylated by BceS
• CssR: phosphorylated by CssS
• NatR: phosphorylated by NatK
• PhoP: phosphorylated by PhoR
• ResD: phosphorylated by ResE
• WalR: phosphorylated by WalK
• YbdJ: phosphorylated by YbdK
• YcbL: phosphorylated by YcbM
• YclJ: phosphorylated by YclK
• YkoG: phosphorylated by YkoH
• YrkP: phosphorylated by YrkO
• YvcP: phosphorylated by YvcQ
• YvrHb: phosphorylated by YvrG
• YxdJ: phosphorylated by YxdK
• CheY: phosphorylated by CheA
• CitT: phosphorylated by CitS
• DctR: phosphorylated by DctS
• GlnL: phosphorylated by GlnK
• MalR: phosphorylated by MalK
• LytT: phosphorylated by LytS
• YesN: phosphorylated by YesM
• Spo0F: part of the phosphorelay, phosphorylated by KinA, KinB, KinC, KinD, or KinE
• Spo0A: part of the phosphorelay, phosphorylated by Spo0B

Phosphorylation on a Cys residue: Enzyme IIB components of the PTS

• PtsG: glucose permease, EIICBA: phosphorylated by PtsG-IIA domain
• GamP: glucosamine permease, EIICBA: phosphorylated by GamP-IIA domain
• MurP: N-acetyl muramic acid-specific phosphotransferase system, EIIBC: likely phosphorylated by PtsG-IIA domain
• SacP: sucrose permease (high affinity): phosphorylated by PtsG-IIA domain
• SacY: sucrose permease (low affinity): phosphorylated by PtsG-IIA domain
• MtlA: mannitol permease: phosphorylated by MtlF
• GmuB: galactomannan permease: phosphorylated by GmuA
• TreP: trehalose permease: phosphorylated by PtsG-IIA domain
• MalP: maltose permease: likely phosphorylated by PtsG-IIA domain
• FruA: fructose permease: phosphorylated by FruA-IIA domain
• ManP: mannose permease: phosphorylated by ManP-IIA domain
• LicB: lichenan permease: phosphorylated by LicA
• BglP: ß-glucoside permease: phosphorylated by BglP-IIA domain

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
  • MtlF: mannitol permease: phosphorylated by HPr
  • GmuA: galactomannan permease: phosphorylated by HPr
  • MalP: maltose permease: phosphorylated by HPr
  • FruA: fructose permease: phosphorylated by HPr
  • ManP: mannose permease: phosphorylated by HPr
  • LevD: fructose permease: phosphorylated by HPr
  • LevE: fructose permease: phosphorylated by LevD
  • LicA: lichenan permease: phosphorylated by HPr
  • BglP: ß-glucoside permease
  • YpqE: unknown EIIA component: phosphorylated by HPr
  • YyzE: truncated PTS IIA protein: might perhaps be phosphorylated by HPr

• 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

• Protein kinases of two-component systems (These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation).)
  • ComP
  • DegS
  • DesK
  • LiaS
  • YdfH
  • YfiJ
  • YhcY
  • YvfT
  • YxjM
  • BceS
  • CssS
  • NatK
  • PhoR
  • ResE
  • WalK
  • YbdK
  • YcbM
  • YclK
  • YkoH
  • YrkO
  • YvcQ
  • YvrG
  • YxdK
  • CheA
  • CitS
  • DctS
  • GlnK
  • MalK
  • LytS
  • YesM
  • YwpD
  • KinA
  • KinB
  • KinC
  • KinD
  • KinE
  • Spo0B: part of the phosphorelay, phosphorylated by Spo0F

Phosphorylation on a Ser residue

• Crh: phosphorylated by HPrK
• Hpr: phosphorylated by HPrK
• AhpF Macek et al., 2007
• AroA Macek et al., 2007
• Asd Macek et al., 2007
• CitH Macek et al., 2007
• CitZ Macek et al., 2007

Phosphorylation on a Thr residue

• LtaS

Phosphorylation on a Tyr residue

• AhpF Macek et al., 2007
• Asd Macek et al., 2007

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)