Literature summary for 2.7.7.101 extracted from

Naue, N.; Beerbaum, M.; Bogutzki, A.; Schmieder, P.; Curth, U.
The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein (2013), Nucleic Acids Res., 41, 4507-4517 .

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Protein Variants

Protein Variants	Comment	Organism
K447A	interaction of mutant with SSB is severely impaired	Escherichia coli
K478A	mutant shows binding affinities to SSB similar to wild-type DnaG C-terminus	Escherichia coli
K518A	interaction of mutant with SSB is severely impaired	Escherichia coli
K528A	mutant shows binding affinities to SSB similar to wild-type DnaG C-terminus	Escherichia coli
R452A	interaction of mutant with SSB is severely impaired	Escherichia coli
T450A	mutant shows a significant decrease in affinity to SSB	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABS5	-	-

General Information

General Information	Comment	Organism
physiological function	the interaction of single-stranded DNA-binding protein SSB and primase is mediated by the C-terminus of SSB. An array of conserved amino acids on DnaG C-terminus forms a hydrophobic pocket surrounded by basic residues, involved in the interaction with SSB	Escherichia coli

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Release 2023.1 (January 2023)