Difference between revisions of "Phosphoproteins"

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(Phosphoproteins in B. subtilis)
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* [[ptsH|Hpr]]: phosphorylated by [[HPrK]]
 
* [[ptsH|Hpr]]: phosphorylated by [[HPrK]]
 
* [[AhpF]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]  
 
* [[AhpF]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]  
 +
* [[AroA]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 +
* [[Asd]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 +
* [[CitH]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 +
* [[CitZ]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
  
 
===Phosphorylation on a Thr residue===
 
===Phosphorylation on a Thr residue===
 
* [[LtaS]]
 
* [[LtaS]]
 +
 +
===Phosphorylation on a Tyr residue===
 +
* [[AhpF]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
 +
* [[Asd]] [http://www.ncbi.nlm.nih.gov/pubmed/17218307 Macek ''et al''., 2007]
  
 
==Related Lists==
 
==Related Lists==

Revision as of 19:54, 21 January 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
  • 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

Phosphorylation on a Ser residue

Phosphorylation on a Thr residue

Phosphorylation on a Tyr residue

Related Lists

Original papers on the B. subtilis phosphoproteome


Reviews