Literature summary for 3.4.21.53 extracted from

Lee, A.Y.; Hsu, C.H.; Wu, S.H.
Functional domains of Brevibacillus thermoruber lon protease for oligomerization and DNA binding: role of N-terminal and sensor and substrate discrimination domains (2004), J. Biol. Chem., 279, 34903-34912.

Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment)	Organism
-	Brevibacillus thermoruber

Protein Variants

Protein Variants	Comment	Organism
additional information	design of truncated enzyme mutants. N-terminal domain is essential for oligomerization. Truncation of N-terminal domain also leads to inactivation of proteolytic, ATPase, and chaperone-like activities of enzyme but retains the DNA-binding activity	Brevibacillus thermoruber

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
90000	-	x * 90000, SDS-PAGE	Brevibacillus thermoruber

Organism

Organism	UniProt	Comment	Textmining
Brevibacillus thermoruber	Q84FG5	stain WR-249	-
Brevibacillus thermoruber WR-249	Q84FG5	stain WR-249	-

Subunits

Subunits	Comment	Organism
?	x * 90000, SDS-PAGE	Brevibacillus thermoruber

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Release 2023.1 (January 2023)