Literature summary for 3.4.21.107 extracted from

Jiang, J.; Zhang, X.; Chen, Y.; Wu, Y.; Zhou, Z.H.; Chang, Z.; Sui, S.F.
Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins (2008), Proc. Natl. Acad. Sci. USA, 105, 11939-11944.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed as a C-terminal his-tagged fusion protein	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
DELTA360-448	mutant lacking the PDZ2 domain. Results of gel filtration reveal that the removal of the whole PDZ2 domain, results in the formation of only trimers that form neither the hexamers nor the 12- or 24-mers. Such a mutant trimeric form of DegP exhibits both chaperone-like and protease activities at a level comparable to that of the wild-type protein. Mutant shows no concentration effect compared to wild-type	Escherichia coli
DELTA440-448	the removal of the beta26 strand on the C terminus of the PDZ2 domain (residues 440-448), which is shown to directly interact with the neighboring PDZ1 domain, does not disrupt the formation of DegP hexamers but prevents their conversion to the 12- or 24-mers. Mutant protein exhibits significantly lower chaperone-like and protease activity, suggesting an inhibitory role of the PDZ2 domain for DegP to exhibit chaperone and protease activities. Mutant shows no concentration effect compared to wild-type	Escherichia coli
S210A	experimental studies are carried out using protease deficient mutant	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	DegP protease exhibits a concentration effect: an 8fold increase in the concentration of DegP results in an 2.4fold increase in the specific protease activity	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-casein + H2O	-	Escherichia coli	?	-	?
Lysozyme + H2O	-	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
multimer	DegP activates its chaperone and protease functions via formation of large cage-like 12- and 24-mers after binding to substrate proteins. Cryo-electron microscopic and biochemical studies reveal that both oligomers are consistently assembled by blocks of DegP trimers, via pairwise PDZ1-PDZ2 interactions between neighboring trimers. Such interactions simultaneously eliminate the inhibitory effects of the PDZ2 domain. Additionally, both DegP oligomers are also observed in extracts of Escherichia. coli cells, strongly implicating their physiological importance	Escherichia coli

Synonyms

Synonyms	Comment	Organism
DegP	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
42	-	substrate-binding using mutant S210A and protease assay	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.6	-	protease assay	Escherichia coli

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Release 2023.1 (January 2023)