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
• CitZ Macek et al., 2007
• CodY Macek et al., 2007
• DegS Macek et al., 2007
• DhbC Macek et al., 2007
• DhbF Macek et al., 2007
• Eno Macek et al., 2007
• Fus Macek et al., 2007

• Mdh Macek et al., 2007

Phosphorylation on a Thr residue

• LtaS
• Drm Macek et al., 2007
• Eno Macek et al., 2007
• FbaA Macek et al., 2007
• Fus Macek et al., 2007
• Hbs Macek et al., 2007
• IspU Macek et al., 2007

Phosphorylation on a Tyr residue

• AhpF Macek et al., 2007
• Asd Macek et al., 2007
• Eno Macek et al., 2007
• InfA Macek et al., 2007
• LctE Macek et al., 2007

Phosphorylation on either a Ser, Thr or Tyr residue

• GapA Macek et al., 2007
• GlgP 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)

Reviews

Daniel C Lee, Zongchao Jia
Emerging structural insights into bacterial tyrosine kinases.
Trends Biochem Sci: 2009, 34(7);351-7
[PubMed:19525115] [WorldCat.org] [DOI] (I p)

Mary Katherine Tarrant, Philip A Cole
The chemical biology of protein phosphorylation.
Annu Rev Biochem: 2009, 78;797-825
[PubMed:19489734] [WorldCat.org] [DOI] (I p)

Paul G Besant, Paul V Attwood
Detection and analysis of protein histidine phosphorylation.
Mol Cell Biochem: 2009, 329(1-2);93-106
[PubMed:19387796] [WorldCat.org] [DOI] (I p)

Emmanuelle Bechet, Sébastien Guiral, Sophie Torres, Ivan Mijakovic, Alain-Jean Cozzone, Christophe Grangeasse
Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes.
Amino Acids: 2009, 37(3);499-507
[PubMed:19189200] [WorldCat.org] [DOI] (I p)

Boris Macek, Matthias Mann, Jesper V Olsen
Global and site-specific quantitative phosphoproteomics: principles and applications.
Annu Rev Pharmacol Toxicol: 2009, 49;199-221
[PubMed:18834307] [WorldCat.org] [DOI] (P p)

Carsten Jers, Boumediene Soufi, Christophe Grangeasse, Josef Deutscher, Ivan Mijakovic
Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks.
Expert Rev Proteomics: 2008, 5(4);619-27
[PubMed:18761471] [WorldCat.org] [DOI] (I p)

Boumediene Soufi, Carsten Jers, Mette Erichsen Hansen, Dina Petranovic, Ivan Mijakovic
Insights from site-specific phosphoproteomics in bacteria.
Biochim Biophys Acta: 2008, 1784(1);186-92
[PubMed:17881301] [WorldCat.org] [DOI] (P p)

Christophe Grangeasse, Alain J Cozzone, Josef Deutscher, Ivan Mijakovic
Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology.
Trends Biochem Sci: 2007, 32(2);86-94
[PubMed:17208443] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Dina Petranovic, Nunzio Bottini, Josef Deutscher, Peter Ruhdal Jensen
Protein-tyrosine phosphorylation in Bacillus subtilis.
J Mol Microbiol Biotechnol: 2005, 9(3-4);189-97
[PubMed:16415592] [WorldCat.org] [DOI] (P p)

Josef Deutscher, Milton H Saier
Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.
J Mol Microbiol Biotechnol: 2005, 9(3-4);125-31
[PubMed:16415586] [WorldCat.org] [DOI] (P p)

Liang Shi
Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions.
Front Biosci: 2004, 9;1382-97
[PubMed:14977554] [WorldCat.org] [DOI] (I e)

Alain J Cozzone, Christophe Grangeasse, Patricia Doublet, Bertrand Duclos
Protein phosphorylation on tyrosine in bacteria.
Arch Microbiol: 2004, 181(3);171-81
[PubMed:14745484] [WorldCat.org] [DOI] (P p)

Susanne Klumpp, Josef Krieglstein
Phosphorylation and dephosphorylation of histidine residues in proteins.
Eur J Biochem: 2002, 269(4);1067-71
[PubMed:11856347] [WorldCat.org] [DOI] (P p)

H S Cho, J G Pelton, D Yan, S Kustu, D E Wemmer
Phosphoaspartates in bacterial signal transduction.
Curr Opin Struct Biol: 2001, 11(6);679-84
[PubMed:11751048] [WorldCat.org] [DOI] (P p)

C J Bakal, J E Davies
No longer an exclusive club: eukaryotic signalling domains in bacteria.
Trends Cell Biol: 2000, 10(1);32-8
[PubMed:10603474] [WorldCat.org] [DOI] (P p)

P J Kennelly, M Potts
Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation.
J Bacteriol: 1996, 178(16);4759-64
[PubMed:8759835] [WorldCat.org] [DOI] (P p)

L N Johnson, D Barford
The effects of phosphorylation on the structure and function of proteins.
Annu Rev Biophys Biomol Struct: 1993, 22;199-232
[PubMed:8347989] [WorldCat.org] [DOI] (P p)

R B Bourret, K A Borkovich, M I Simon
Signal transduction pathways involving protein phosphorylation in prokaryotes.
Annu Rev Biochem: 1991, 60;401-41
[PubMed:1883200] [WorldCat.org] [DOI] (P p)