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Literature summary for 3.4.21.B30 extracted from

  • Neher, S.B.; Sauer, R.T.; Baker, T.A.
    Distinct peptide signals in the UmuD and UmuD' subunits of UmuD/D' mediate tethering and substrate processing by the ClpXP protease (2003), Proc. Natl. Acad. Sci. USA, 100, 13219-13224.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B30

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
E11V/I12V/V13K supports ClpXP degradation of UmuD' Escherichia coli
R37A when mutation is present in the UmuD' subunit of a UmuD/D' heterodimer it causes this subunit to be degraded substantially more slowly than its wild-type counterpart, when the mutation is present in the UmuD subunit of the heterodimer degradation of the UmuD' subunit occurs as efficiently as with the wild-type enzyme 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification processing of UmuD to the shorter, but mutagenically active UmuD' by ClpXP protease, UmuD' must form a heterodimer with its unabbreviated precursor for efficient degradation, UmuD2 homodimers are degraded with an efficiency similar to the UmuD' subunit of the UmuD/UmuD' heterodimer 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 Escherichia coli ?
-
 ?