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Literature summary for 3.4.21.B30 extracted from

  • Ollivierre, J.N.; Budil, D.E.; Beuning, P.J.
    Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD (2011), Mol. Biosyst., 7, 3183-3186.
    View publication on PubMed
Search for more literature for 3.4.21.B30

Protein Variants

Protein Variants Comment Organism
A31C UmuD’ mutant Escherichia coli
S60A active-site UmuD mutant Escherichia coli
T14A/L17A/F18A the mutant is a non-cleavable variant of UmuD Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the damage-induced RecA:ssDNA nucleoprotein filament facilitates autocleavage of the N-terminal 24-amino acids of UmuD2 to yield UmuD'2, the form that enables mutagenesis ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the damage-induced RecA:ssDNA nucleoprotein filament facilitates autocleavage of the N-terminal 24-amino acids of UmuD2 to yield UmuD'2, the form that enables mutagenesis Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
homodimer UmuD2 Escherichia coli

Synonyms

Synonyms Comment Organism
UmuD
-
 Escherichia coli
UmuD'
-
 Escherichia coli
UmuD2
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 Escherichia coli

General Information

General Information Comment Organism
physiological function UmuD2 is the initial umuD gene product that appears after induction of the SOS response. It is involved in regulating mutagenesis as part of the tightly controlled SOS response Escherichia coli