Literature summary for 2.7.7.101 extracted from

Ayora, S.; Langer, U.; Alonso, J.
Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex (1998), FEBS Lett., 439, 59-62 .

No PubMed abstract available

Search for more literature for 2.7.7.101

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
69000	-	gel filtration	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
overproduced recombinant polypeptide is insoluble, aggregates can be dissolved in the presence of 3 M urea	Bacillus subtilis

Subunits

Subunits	Comment	Organism
monomer	1 * 68800, calculated from sequence, 1 * 69000, SDS-PAGE	Bacillus subtilis

General Information

General Information	Comment	Organism
physiological function	DnaG physically interacts with bacteriophage SPP1 hexameric helicase G40P (G40P6) in the absence of ATP. The presence of DnaG in the reaction mixture increases the helicase activity of G40P6 about 3fold, but not the ATPase activity	Bacillus subtilis

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Release 2023.1 (January 2023)