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Literature summary for 3.4.21.B30 extracted from

  • Gonzalez, M.; Frank, E.G.; Levine, A.S.; Woodgate, R.
    Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis (1998), Genes Dev., 12, 3889-3899.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K97A mutant is able to undergo intermolecular cleavage, but not intramolecular self-cleavage Escherichia coli

General Stability

General Stability Organism
highly purified UmuD is specifically degraded in vitro by Lon protease in an ATP-dependent manner, UmuD' is insensitive to proteolysis by Lon Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli role in SOS mutagenesis ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification UmuD is posttranslationally activated by cleavage yielding UmuD' Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information role in SOS mutagenesis Escherichia coli ?
-
?