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Literature summary extracted from

  • McCleary, W.R.; Zusman, D.R.
    Purification and characterization of the Myxococcus xanthus FrzE protein shows that it has autophosphorylation activity (1990), J. Bacteriol., 172, 6661-6668.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.13.3
-
 Myxococcus xanthus

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Myxococcus xanthus P18769
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.13.3 phosphoprotein autophosphorylation Myxococcus xanthus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.13.3 recombinant FrzE protein is overproduced in Escherichia coli and purified from inclusion bodies Myxococcus xanthus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.13.3 additional information FrzE is clearly present during vegetative growth and at much lower levels during development Myxococcus xanthus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 protein + ATP autophosphorylation Myxococcus xanthus ?
-
 ?
2.7.13.3 protein + ATP a model of the mechanism of FrzE phosphorylation: autophosphorylation initially occurs at a conserved His residue within the "CheA" domain and then, via an intramolecular transphosphorylation, is transferred to a conserved aspartate residue within the "CheY" domain Myxococcus xanthus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 FrzE
-
 Myxococcus xanthus
2.7.13.3 gliding motility regulatory protein
-
 Myxococcus xanthus