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, interaction properties and/ or localization.

Parent category	6. Groups of genes
Neighbouring categories	6.1. Essential genes 6.2. Membrane proteins 6.3. GTP-binding proteins 6.4. Phosphoproteins 6.5. Universally conserved proteins 6.6. Poorly characterized/ putative enzymes 6.7. Proteins of unknown function 6.8. Short peptides 6.9. ncRNA 6.10. Pseudogenes
Related categories	none
Overview on the categories (Excel file) All genes and their categories (Excel file)

Phosphoproteins in B. subtilis

Phosphorylation on an Arg residue

• CtsR, phosphorylated by McsB

Phosphorylation on an Asp residue: Response regulators of two-component systems

• BceR: phosphorylated by BceS
• CheB: phosphorylated by CheA
• CheV: phosphorylated by CheA
• CheY: phosphorylated by CheA
• CitT: phosphorylated by CitS

• ComA: phosphorylated by ComP
• CssR: phosphorylated by CssS
• DctR: phosphorylated by DctS
• DegU: phosphorylated by DegS
• DesR: phosphorylated by DesK

• GlnL: phosphorylated by GlnK
• LiaR: phosphorylated by LiaS
• LytT: phosphorylated by LytS
• MalR: phosphorylated by MalK
• NatR: phosphorylated by NatK

• PhoP: phosphorylated by PhoR
• ResD: phosphorylated by ResE
• Spo0A: part of the phosphorelay, phosphorylated by Spo0B
• Spo0F: part of the phosphorelay, phosphorylated by KinA, KinB, KinC, KinD, or KinE
• WalR: phosphorylated by WalK

• YbdJ: phosphorylated by YbdK
• YcbL: phosphorylated by YcbM
• YclJ: phosphorylated by YclK
• YdfI: phosphorylated by YdfH
• YesN: phosphorylated by YesM

• YfiK: phosphorylated by YfiJ
• YhcZ: phosphorylated by YhcY
• YkoG: phosphorylated by YkoH
• YrkP: phosphorylated by YrkO
• YvcP: phosphorylated by YvcQ

• YvfU: phosphorylated by YvfT
• YvrHb: phosphorylated by YvrG
• YxdJ: phosphorylated by YxdK
• YxjL: phosphorylated by YxjM

Phosphorylation on a Cys residue

• PRD-type regulator containing a IIB-like domain
  • MtlR: phosphorylated by MtlF

• 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
  • SacX: 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
  • NagP: N-acetylglucosamine permease: phosphorylated by PtsG-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).)
  • BceS
  • CheA
  • CitS
  • ComP
  • CssS

• • DctS
  • DegS
  • DesK
  • GlnK
  • KinA

• • KinB
  • KinC
  • KinD
  • KinE
  • LiaS

• • LytS
  • MalK
  • NatK
  • PhoR
  • ResE

• • Spo0B: part of the phosphorelay, phosphorylated by Spo0F
  • WalK
  • YbdK
  • YcbM
  • YclK

• • YdfH
  • YesM
  • YfiJ
  • YhcY
  • YkoH

• • YrkO
  • YvcQ
  • YvfT
  • YvrG
  • YwpD

• • YxdK
  • YxjM

Phosphorylation on a Ser residue

• Crh: phosphorylated by HPrK
• Hpr: phosphorylated by HPrK
• AbrB Soufi et al., 2010
• 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
• FusA Macek et al., 2007
• GerR Soufi et al., 2010
• GlmM Macek et al., 2007

Eymannet al., 2007

• GroES Soufi et al., 2010
• GyrB Soufi et al., 2010
• IlvC Soufi et al., 2010
• LicB Macek et al., 2007
• ManP Macek et al., 2007

• Mdh Macek et al., 2007
• MetS Soufi et al., 2010
• MtlA Macek et al., 2007
• Ndk Macek et al., 2007
• PdhB Macek et al., 2007

• Pgk Macek et al., 2007
• Pgm Macek et al., 2007
• PnbA Macek et al., 2007
• PupG Macek et al., 2007
• Enzyme I Macek et al., 2007

• Pyk Macek et al., 2007 Eymannet al., 2007
• PyrB Macek et al., 2007
• RecA Soufi et al., 2010
• RocF Soufi et al., 2010
• RsbRC Macek et al., 2007

• RsbS Macek et al., 2007
• RsbV Macek et al., 2007 Eymannet al., 2007
• SpoIIAA Macek et al., 2007
• SpoVG Macek et al., 2007
• SrfAA Macek et al., 2007

• SrfAB Macek et al., 2007
• SrfAC Macek et al., 2007
• SucC Macek et al., 2007
• TagE Macek et al., 2007
• ThiC Soufi et al., 2010

• Tpi Macek et al., 2007
• TrmK Macek et al., 2007
• Tsf Macek et al., 2007
• MurQ Macek et al., 2007
• YcnE Macek et al., 2007

• YerA Macek et al., 2007
• YfjC Soufi et al., 2010
• YfkK Macek et al., 2007
• YjbK Soufi et al., 2010
• YpfD Macek et al., 2007

• YpoC Macek et al., 2007
• YqbO Macek et al., 2007
• YtnP Macek et al., 2007
• YukF Soufi et al., 2010
• YurJ Soufi et al., 2010

• YwfI Macek et al., 2007
• YwjH Macek et al., 2007
• YwrJ Soufi et al., 2010

Phosphorylation on a Thr residue

• LtaS
• AroA Eymannet al., 2007
• Drm Macek et al., 2007
• Eno Macek et al., 2007
• FbaA Macek et al., 2007
• FusA Macek et al., 2007
• GndA Macek et al., 2007
• Hbs Macek et al., 2007
• Ndk Macek et al., 2007
• OppA Macek et al., 2007
• Pgi Macek et al., 2007
• Pgk Macek et al., 2007
• PrkC Macek et al., 2007
• PrkD Pietacket al., 2010
• RsbR Macek et al., 2007 Eymannet al., 2007
• RsbRB Eymannet al., 2007 Macek et al., 2007
• RsbRC Macek et al., 2007
• RsbRD Macek et al., 2007 Eymannet al., 2007
• SodA Macek et al., 2007
• TyrZ Soufi et al., 2010
• YdcC Soufi et al., 2010

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
• Ldh Macek et al., 2007
• OppA Macek et al., 2007
• PtkA Soufi et al., 2010
• SsbA Mijakovic et al., 2006
• SsbB Mijakovic et al., 2006
• ThiC Soufi et al., 2010
• TuaD Mijakovic et al., 2003
• Ugd Mijakovic et al., 2003, Macek et al., 2007
• YjoA Macek et al., 2007
• YnfE Macek et al., 2007
• YorK Macek et al., 2007
• YvyG Macek et al., 2007

Phosphorylation on either a Ser, Thr or Tyr residue

• AhpC Levine et al., 2007
• AlsD Levine et al., 2007
• AspS Levine et al., 2007
• AtpA Levine et al., 2007
• AtpD Levine et al., 2007
• DnaK Eymannet al., 2007
• DppA Levine et al., 2007
• GapA Macek et al., 2007 Eymannet al., 2007
• GlgP Macek et al., 2007
• GlnA Levine et al., 2007
• GlyA Levine et al., 2007 Eymannet al., 2007
• GpsB Macek et al., 2007
• GroEL Levine et al., 2007 Eymannet al., 2007
• GtaB Levine et al., 2007
• GuaB Eymannet al., 2007
• Icd Levine et al., 2007 Eymannet al., 2007
• MetE Eymannet al., 2007
• PdhD Eymannet al., 2007
• PdxS Levine et al., 2007 Eymannet al., 2007
• PgcA Levine et al., 2007 Eymannet al., 2007
• PstS Levine et al., 2007
• Pta Macek et al., 2007
• RocA Macek et al., 2007
• SdhA Levine et al., 2007 Eymannet al., 2007
• SucD Macek et al., 2007
• ThiG Eymannet al., 2007
• Tig Levine et al., 2007
• Tkt Levine et al., 2007
• TufA Levine et al., 2007 Eymannet al., 2007
• YerB Macek et al., 2007
• YfiY Macek et al., 2007
• YfjR Levine et al., 2007
• YfnI Macek et al., 2007
• YhfK Levine et al., 2007
• YoxD Levine et al., 2007
• YsnF Levine et al., 2007
• YtaG Levine et al., 2007
• YtxJ Macek et al., 2007
• SufC Levine et al., 2007
• YxxG Macek et al., 2007
• Zur Levine et al., 2007

Related Lists

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

Reviews

Jörg Stülke
More than just activity control: phosphorylation may control all aspects of a protein's properties.
Mol Microbiol: 2010, 77(2);273-5
[PubMed:20497498] [WorldCat.org] [DOI] (I p)

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)