Difference between revisions of "Phosphoproteins"

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(Phosphorylation on a His residue)
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* Protein kinases of [[two-component systems]] (These kinases are dimeric proteins. Phosphorylation occurs from one subunit to the other (not quite an autophosphorylation).)
 
* 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]]
 
** [[ComP]]
 +
** [[CssS]]
 +
 +
** [[DctS]]
 
** [[DegS]]
 
** [[DegS]]
 
** [[DesK]]
 
** [[DesK]]
 +
** [[GlnK]]
 +
** [[KinA]]
 +
 +
** [[KinB]]
 +
** [[KinC]]
 +
** [[KinD]]
 +
** [[KinE]]
 
** [[LiaS]]
 
** [[LiaS]]
** [[YdfH]]
+
 
** [[YfiJ]]
+
** [[LytS]]
** [[YhcY]]
+
** [[MalK]]
** [[YvfT]]
 
** [[YxjM]]
 
** [[BceS]]
 
** [[CssS]]
 
 
** [[NatK]]
 
** [[NatK]]
 
** [[PhoR]]
 
** [[PhoR]]
 
** [[ResE]]
 
** [[ResE]]
 +
 +
** [[Spo0B]]: part of the [[phosphorelay]], phosphorylated by [[Spo0F]]
 
** [[WalK]]
 
** [[WalK]]
 
** [[YbdK]]
 
** [[YbdK]]
 
** [[YcbM]]
 
** [[YcbM]]
 
** [[YclK]]
 
** [[YclK]]
 +
 +
** [[YdfH]]
 +
** [[YesM]]
 +
** [[YfiJ]]
 +
** [[YhcY]]
 
** [[YkoH]]
 
** [[YkoH]]
 +
 
** [[YrkO]]
 
** [[YrkO]]
 
** [[YvcQ]]
 
** [[YvcQ]]
 +
** [[YvfT]]
 
** [[YvrG]]
 
** [[YvrG]]
 +
** [[YwpD]]
 +
 
** [[YxdK]]
 
** [[YxdK]]
** [[CheA]]
+
** [[YxjM]]
** [[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 Ser residue===

Revision as of 16:08, 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 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