Literature summary 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.

Activating Compound

EC Number	Activating Compound	Comment	Organism
3.4.21.107	DKVLVVWAGQQ	MalS-derived peptide sequence	Escherichia coli
3.4.21.107	DNRNGNVYDF	-	Escherichia coli
3.4.21.107	DNRNGNVYFF	thermodynamic binding affinities of the peptide	Escherichia coli
3.4.21.107	DNRNGNVYGF	-	Escherichia coli
3.4.21.107	DNRNGNVYIF	-	Escherichia coli
3.4.21.107	DNRNGNVYKF	-	Escherichia coli
3.4.21.107	DNRNGNVYLF	thermodynamic binding affinities of the peptide	Escherichia coli
3.4.21.107	DNRNGNVYQF	-	Escherichia coli
3.4.21.107	DNRNGNVYSF	-	Escherichia coli
3.4.21.107	DNRNGNVYWF	-	Escherichia coli
3.4.21.107	DNRNGNVYYF	-	Escherichia coli
3.4.21.107	IVALGLVYQF	OmpC-derived peptide sequence	Escherichia coli
3.4.21.107	additional information	allosteric activation of DegP by stress signals during bacterial protein quality control, DegP activation is based on an interaction of the activating peptide with PDZ domains	Escherichia coli
3.4.21.107	YTMKAAGLGK	PhoA-derived peptide sequence	Escherichia coli
3.4.21.108	casein	2.5fold activation	Bacteria
3.4.21.108	DKVLVVWAGQQ	full-length denatured alpha-amylase, as well as alpha-amylase fragments and the C-terminus of alpha-amylase, amplify DegP proteolysis	Bacteria
3.4.21.108	DNRNGNVYDF	-	Bacteria
3.4.21.108	DNRNGNVYFF	2.5fold activation	Bacteria
3.4.21.108	DNRNGNVYGF	-	Bacteria
3.4.21.108	DNRNGNVYIF	-	Bacteria
3.4.21.108	DNRNGNVYKF	-	Bacteria
3.4.21.108	DNRNGNVYLF	-	Bacteria
3.4.21.108	DNRNGNVYQF	1.5fold activation	Bacteria
3.4.21.108	DNRNGNVYSF	-	Bacteria
3.4.21.108	DNRNGNVYWF	2fold activation	Bacteria
3.4.21.108	DNRNGNVYYF	-	Bacteria
3.4.21.108	IVALGLVYQF	outer membrane porin C, 3fold activation	Bacteria
3.4.21.108	YTMKAAGLGK	alkaline phosphatase A	Bacteria

Application

EC Number	Application	Comment	Organism
3.4.21.108	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

EC Number	Protein Variants	Comment	Organism
3.4.21.108	R262A	completely abolishes proteolytic activation	Bacteria
3.4.21.108	V328S	completely abolishes proteolytic activation	Bacteria

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3.4.21.107	additional information	Escherichia coli	allosteric activation of DegP by stress signals during bacterial protein quality control, regulation mechanism, pathway scheme, overview	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.21.107	Escherichia coli	-	-	-
3.4.21.108	Bacteria	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
3.4.21.107	additional information	allosteric activation of DegP by stress signals during bacterial protein quality control, regulation mechanism, pathway scheme, overview	Escherichia coli	?	-	?
3.4.21.108	additional information	no cleavage of STDGGV-para-nitroaniline and SKAKGGEEPLPEGV-para-nitroaniline	Bacteria	?	-	?
3.4.21.108	SPMFKGV-p-nitroanilide + H2O	-	Bacteria	?	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.4.21.107	bacterial PQC factor	-	Escherichia coli
3.4.21.107	DegP	-	Escherichia coli
3.4.21.107	HtrA protease	-	Escherichia coli
3.4.21.108	DegP	-	Bacteria
3.4.21.108	HtrA protease	-	Bacteria

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
3.4.21.108	0.56	-	SPMFKGV-para-nitroaniline	-	Bacteria

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.4.21.107	8	-	activation assay at	Escherichia coli