Difference between revisions of "Phosphoproteins"

From SubtiWiki
Jump to: navigation, search
(→‎Phosphorylation on a Ser residue)
(→‎Phosphorylation on a Thr residue)
Line 183: Line 183:
 
* [[GndA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[GndA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[Hbs]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[Hbs]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
−
* [[IspU]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
 
* [[Ndk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[Ndk]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[OppA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[OppA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
Line 191: Line 190:
 
* [[PrkD]] [http://www.ncbi.nlm.nih.gov/pubmed/20389117 Pietack''et al''., 2010]
 
* [[PrkD]] [http://www.ncbi.nlm.nih.gov/pubmed/20389117 Pietack''et al''., 2010]
 
* [[RsbR]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]
 
* [[RsbR]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]
−
* [[RsbRB]] [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]
+
* [[RsbRB]] [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[RsbRC]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[RsbRC]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[RsbRD]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]
 
* [[RsbRD]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007] [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]

Revision as of 18:01, 21 April 2010

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

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

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
  • 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

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)


Reviews

Retrieved from "http://subtiwiki.uni-goettingen.de/wiki//index.php?title=Phosphoproteins&oldid=121746"