Literature summary for 3.4.21.108 extracted from

Meltzer, M.; Hasenbein, S.; Hauske, P.; Kucz, N.; Merdanovic, M.; Grau, S.; Beil, A.; Jones, D.; Krojer, T.; Clausen, T.; Ehrmann, M.; Kaiser, M.
Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control (2008), Angew. Chem. Int. Ed. Engl., 47, 1332-1334.

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Activating Compound

Activating Compound	Comment	Organism	Structure
casein	2.5fold activation	Bacteria
DKVLVVWAGQQ	full-length denatured alpha-amylase, as well as alpha-amylase fragments and the C-terminus of alpha-amylase, amplify DegP proteolysis	Bacteria
DNRNGNVYDF	-	Bacteria
DNRNGNVYFF	2.5fold activation	Bacteria
DNRNGNVYGF	-	Bacteria
DNRNGNVYIF	-	Bacteria
DNRNGNVYKF	-	Bacteria
DNRNGNVYLF	-	Bacteria
DNRNGNVYQF	1.5fold activation	Bacteria
DNRNGNVYSF	-	Bacteria
DNRNGNVYWF	2fold activation	Bacteria
DNRNGNVYYF	-	Bacteria
IVALGLVYQF	outer membrane porin C, 3fold activation	Bacteria
YTMKAAGLGK	alkaline phosphatase A	Bacteria

Application

Application	Comment	Organism
additional information	the bacterial protein quality control factor DegP is allosterically regulated by model peptides mimicking cellular stress signals. Strategy for the development of antimicrobials	Bacteria

Protein Variants

Protein Variants	Comment	Organism
R262A	completely abolishes proteolytic activation	Bacteria
V328S	completely abolishes proteolytic activation	Bacteria

Organism

Organism	UniProt	Comment	Textmining
Bacteria	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	no cleavage of STDGGV-para-nitroaniline and SKAKGGEEPLPEGV-para-nitroaniline	Bacteria	?	-	?
SPMFKGV-p-nitroanilide + H2O	-	Bacteria	?	-	?

Synonyms

Synonyms	Comment	Organism
DegP	-	Bacteria
HtrA protease	-	Bacteria

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.56	-	SPMFKGV-para-nitroaniline	-	Bacteria

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Release 2026.1 (March 2026)