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Literature summary extracted from

  • Wu, J.; Ohta, N.; Zhao, J.L.; Newton, A.
    A novel bacterial tyrosine kinase essential for cell division and differentiation (1999), Proc. Natl. Acad. Sci. USA, 96, 13068-13073.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.13.3 ATP + a protein Caulobacter vibrioides the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division ADP + a phosphoprotein
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Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Caulobacter vibrioides Q9RQQ9
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 ATP + a protein the tyrosine kinase DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA, the enzyme is essential for cell viability and division Caulobacter vibrioides ADP + a phosphoprotein
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2.7.13.3 protein + ATP DivL protein is homologous to the ubiquitous bacterial histidine protein kinases, it differs from previously studied members of this protein kinase family in that it contains a tyrosine residue Tyr550 in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation. DivL is autophosphorylated on Tyr-550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle Caulobacter vibrioides ?
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Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 sensor protein divL
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 Caulobacter vibrioides