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Literature summary for 3.4.21.107 extracted from

  • Meltzer, M.; Hasenbein, S.; Mamant, N.; Merdanovic, M.; Poepsel, S.; Hauske, P.; Kaiser, M.; Huber, R.; Krojer, T.; Clausen, T.; Ehrmann, M.
    Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli (2009), Res. Microbiol., 160, 660-666.
    View publication on PubMed
Search for more literature for 3.4.21.107

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli when unfolded proteins bind to CpxP, DegP efficiently degrades this protein complex ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information when unfolded proteins bind to CpxP, DegP efficiently degrades this protein complex Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Escherichia coli
tetracosamer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
DegP
-
 Escherichia coli
high temperature requirement A
-
 Escherichia coli
HtrA
-
 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli RpoE is released from the membrane to function as a sigma factor that induces degP expression. On the protein level, DegP activity is upregulated by C-termini of omps as well as misfolded periplasmic proteins up

General Information

General Information Comment Organism
physiological function DegP can act as a chaperone and a protease at the same time. Deg P is a key player in extracytoplasmic protein quality control and exhibits features of a protective factor during protein folding stress. As a chaperone, DegP refolds periplasmic amylase MalS and the artificial substrate citrate synthase Escherichia coli