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

Phosphorylation on a Thr residue

Phosphorylation on a Tyr residue

Phosphorylation on either a Ser, Thr or Tyr residue

Related Lists

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)

Phosphoproteins

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