Literature summary for 3.4.21.53 extracted from

Chir, J.L.; Liao, J.H.; Lin, Y.C.; Wu, S.H.
The N-terminal sequence after residue 247 plays an important role in structure and function of Lon protease from Brevibacillus thermoruber WR-249 (2009), Biochem. Biophys. Res. Commun., 382, 762-765.

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Protein Variants

Protein Variants	Comment	Organism
additional information	construction of randomly chosen N-terminally truncated mutants. Mutants lacking amino acids from 1 to 247 of N-terminus retain significant peptidase and ATPase activities, but lose 90% of protease activity. Further truncation of the protein results in the loss of all three activities. Mutants lacking amino acids 246-259 or 248-256 also lose all activities and quaternary structure	Brevibacillus thermoruber

Organism

Organism	UniProt	Comment	Textmining
Brevibacillus thermoruber	-	WR-249	-
Brevibacillus thermoruber WR-249	-	WR-249	-

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Release 2023.1 (January 2023)