Literature summary for 3.4.21.B30 extracted from

Murison, D.A.; Timson, R.C.; Koleva, B.N.; Ordazzo, M.; Beuning, P.J.
Identification of the dimer exchange interface of the bacterial DNA damage response protein UmuD (2017), Biochemistry, 56, 4773-4785 .

Search for more literature for 3.4.21.B30

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AG11	-	-
Escherichia coli K12	P0AG11	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	full-length UmuD is expressed as a homodimer of 139-amino-acid subunits, which eventually cleaves its N-terminal 24 amino acids to form UmuD'. The cleavage product UmuD' and UmuC form the Y-family polymerase DNA Pol V (UmuD'2C) capable of performing translesion synthesis	Escherichia coli

Subunits

Subunits	Comment	Organism
dimer	UmuD and the cleavage product UmuD' exist as homodimers. Their subunits can readily exchange to form UmuDD' heterodimers preferentially. Heterodimer formation is an essential step in the degradation pathway of UmuD'	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	the umuD gene products are upregulated after DNA damage and play roles in both nonmutagenic and mutagenic aspects of the SOS response	Escherichia coli

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Release 2023.1 (January 2023)