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Literature summary for 3.4.21.B30 extracted from

  • Sutton, M.D.; Kim, M.; Walker, G.C.
    Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage (2001), J. Bacteriol., 183, 347-357.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Protein Variants

Protein Variants Comment Organism
L101G/R102G mutant enzyme is defective in RecA-ssDNA-facilitated self-cleavage in vivo, can undergo RecA-ssDNA-facilitated cleavage in vitro, can interact directly with the RecA-ssDNA nucleoprotein filament in vitro, and is active in SOS mutagenesis in vivo Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis ?
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification UmuD protein is activated by a RecA-single-stranded DNA-facilitated self-cleavage event that serves to remove its amino-terminal 24 residues to yield 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 UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis Escherichia coli ?
-
?