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Literature summary for 2.7.11.1 extracted from

  • Fiuza, M.; Canova, M.J.; Zanella-Cleon, I.; Becchi, M.; Cozzone, A.J.; Mateos, L.M.; Kremer, L.; Gil, J.A.; Molle, V.
    From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division (2008), J. Biol. Chem., 283, 18099-18112.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
PknA activation of PknG is part of a phosphorylation cascade mechanism that relies on PknA activity Corynebacterium glutamicum

Application

Application Comment Organism
molecular biology pknA and pknB are key players in signal transduction pathways for the regulation of the cell shape and both are essential for sustaining corynebacterial growth Corynebacterium glutamicum

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
additional information conditional mutants of pknA or pknB are created, leading to partial depletion of PknA or PknB. This results in elongated cells, indicative of a cell division defect. Moreover, overexpression of PknA or PknB in Corynebacterium glutamicum results in a lack of apical growth and therefore a coccoid-like morphology Corynebacterium glutamicum
additional information disruption of either pknL or pknG results in viable mutants presenting a typical cell morphology and growth rate Corynebacterium glutamicum
additional information null mutant can not be generated, indicating that PknA gene is essential Corynebacterium glutamicum
additional information null mutant can not be generated, indicating that PknB gene is essential Corynebacterium glutamicum

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum A0A160PV21
-
-
Corynebacterium glutamicum Q8NM29
-
-
Corynebacterium glutamicum Q8NU97
-
-
Corynebacterium glutamicum Q8NU98
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein enzyme does not possess autokinase activity. Phosphorylated residues by PknA: Thr451, Thr787 Corynebacterium glutamicum
phosphoprotein enzyme possesses autokinase activity. Phosphorylated residues: Thr123, Thr304, Thr308, Thr309, Thr382, Ser384, Ser387, Thr392 Corynebacterium glutamicum
phosphoprotein enzyme possesses autokinase activity. Phosphorylated residues: Thr169, Thr306, Thr310 Corynebacterium glutamicum
phosphoprotein enzyme possesses autokinase activity. Phosphorylated resiudes: Thr179, Thr181, Ser228, Ser229, Ser231, Thr292, Thr298, Thr319, Thr321 Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + OdhI following phosphorylation by PknA, PknG can transphosphorylate its specific substrate 2-oxoglutarate dehydrogenase inhibitor protein (OdhI) in vitro Corynebacterium glutamicum ADP + phosphorylated-OdhI
-
?
ATP + PknG activation of PknG is part of a phosphorylation cascade mechanism that relies on PknA activity Corynebacterium glutamicum ADP + phosphorylated-PknG
-
?

Synonyms

Synonyms Comment Organism
PknA
-
Corynebacterium glutamicum
PknB
-
Corynebacterium glutamicum
PknG
-
Corynebacterium glutamicum
PknL
-
Corynebacterium glutamicum
serine/threonine protein kinase
-
Corynebacterium glutamicum
StpK
-
Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Corynebacterium glutamicum