Difference between revisions of "Phosphoproteins"

From SubtiWiki
Jump to: navigation, search
(Phosphorylation on a Ser residue)
(Phosphorylation on a Ser residue)
Line 181: Line 181:
 
* [[FusA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[FusA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 
* [[GerR]] [http://www.ncbi.nlm.nih.gov/pubmed/20509597 Soufi ''et al''., 2010]  
 
* [[GerR]] [http://www.ncbi.nlm.nih.gov/pubmed/20509597 Soufi ''et al''., 2010]  
* [[GlmM]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]  
+
* [[GlmM]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]
[http://www.ncbi.nlm.nih.gov/pubmed/17726680 Eymann''et al''., 2007]
 
  
 
* [[GroES]] [http://www.ncbi.nlm.nih.gov/pubmed/20509597 Soufi ''et al''., 2010]  
 
* [[GroES]] [http://www.ncbi.nlm.nih.gov/pubmed/20509597 Soufi ''et al''., 2010]  

Revision as of 15:14, 1 January 2011

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
Neighbouring categories
Related categories

none






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


Reviews