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	protein kinases and phosphatases two-component systems PTS PRD-containing transcription factors phosphorelay response regulator aspartate phosphatases
Overview on the categories (Excel file) All genes and their categories (Excel file)

Phosphoproteins in B. subtilis

Phosphorylation on an Arg residue

CtsR (R55), phosphorylated by McsB
AccD
AhpF
AlaR
AlbF (R17)
Apt
ArgG
AroA
AroF
AtpH
BdhA
BfmBAB (R23)
ClpC
ClpP
ComFA
ComFC
ComGA
ComK
CsoR (R24)
DivIVA
FadB
FliY
FlgN
FrlB
GanA
GapA
GatC
GgaA
GltA
Gmk
GroEL
GtaB
GudB
Hbs
HemB
Hpf
HrcA
Icd
IlvB
IlvC
IolE (R216)
KatA
LeuB
LeuC
LutB
LutC
McsA
Mdh
MelA (R56)
MenB
MntB (R132)
MtnA

MtnK
NadB
Nin
OdhA
OdhB (R300)
OxdC
PdxS
PfkA
PurA
RadC
RecA
RplK
RplN (R17)
RplV (R11)
RplW
RpmEB
RpmGA
RpoB
RpoC
RpsG
RpsH (R47, R72)
RpsI
RpsL
RpsM
RpsN
ScoC
SrfAA (R226)
SrfAB
SsbA
SsbB
ThiC
ThyB
Tig
TufA (R384)
YceE
YciC
YdcI
YdjO
YerA (R14)
YfmG
YheA
YkoM (R89)
YkyB (R26)
YlbN
YloV
YpiF (R4)
YrvO

YtxH
YvfU (R116, R143)
YvrO

YwpJ

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

Phosphorylation on a Thr residue

Phosphorylation on a Tyr residue

Phosphorylation on either a Ser, Thr or Tyr residue

Zur Levine et al., 2007

Original papers on the B. subtilis phosphoproteome

Vaishnavi Ravikumar, Lei Shi, Karsten Krug, Abderahmane Derouiche, Carsten Jers, Charlotte Cousin, Ahasanul Kobir, Ivan Mijakovic, Boris Macek
Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.
Mol Cell Proteomics: 2014, 13(8);1965-78
[PubMed:24390483] [WorldCat.org] [DOI] (I p)

Andreas Schmidt, Débora Broch Trentini, Silvia Spiess, Jakob Fuhrmann, Gustav Ammerer, Karl Mechtler, Tim Clausen
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Mol Cell Proteomics: 2014, 13(2);537-50
[PubMed:24263382] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

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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