Activating Compound | Comment | Organism | Structure |
---|---|---|---|
PknA | activation of PknG is part of a phosphorylation cascade mechanism that relies on PknA activity | Corynebacterium glutamicum |
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 (Comment) | Organism |
---|---|
expressed in Escherichia coli | Corynebacterium glutamicum |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | A0A160PV21 | - |
- |
Corynebacterium glutamicum | Q8NM29 | - |
- |
Corynebacterium glutamicum | Q8NU97 | - |
- |
Corynebacterium glutamicum | Q8NU98 | - |
- |
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 | 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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Corynebacterium glutamicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Corynebacterium glutamicum |