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Literature summary extracted from

  • Subrini, O.; Betton, J.M.
    Assemblies of DegP underlie its dual chaperone and protease function (2009), FEMS Microbiol. Lett., 296, 143-148.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.107 cardiolipin enhances DegP proteolytic activity at high temperatures Escherichia coli K-12
3.4.21.107 phosphatidyl glycerol enhances DegP proteolytic activity at high temperatures Escherichia coli K-12

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.107 S210A proteolytically inactive Escherichia coli K-12

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.107 periplasm
-
Escherichia coli K-12
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.107 outer membrane protein + H2O Escherichia coli K-12
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.107 Escherichia coli K-12 P0C0V0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.107 outer membrane protein + H2O
-
Escherichia coli K-12 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.21.107 homooligomer DegP of Escherichia coli assembles into large homooligomers with an internal cavity combining both chaperone and protease activity Escherichia coli K-12

Synonyms

EC Number Synonyms Comment Organism
3.4.21.107 DegP
-
Escherichia coli K-12
3.4.21.107 HtrA
-
Escherichia coli K-12

General Information

EC Number General Information Comment Organism
3.4.21.107 physiological function DegP is a periplasmic heat-shock protein and a key component of protein quality control in the bacterial envelope. DegP along with the Skp chaperone functions to rescue outer membrane proteins that escape recognition by SurA. At temperatures below 28°C, DegP is able to protect misfolded proteins from forming aggregates, whereas at temperatures above 30°C, misfolded proteins are efficiently degraded by DegP Escherichia coli K-12