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Literature summary for 3.4.21.107 extracted from

  • Baud, C.; Hodak, H.; Willery, E.; Drobecq, H.; Locht, C.; Jamin, M.; Jacob-Dubuisson, F.
    Role of DegP for two-partner secretion in Bordetella (2009), Mol. Microbiol., 74, 315-329.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Bordetella pertussis

Protein Variants

Protein Variants Comment Organism
S237A protease-inactive mutant Bordetella pertussis

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Bordetella pertussis
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
filamentous haemagglutinin precursor + H2O Bordetella pertussis DegP contributes to degrading the filamentous haemagglutinin precursor when it is blocked intracellularly ?
-
?

Organism

Organism UniProt Comment Textmining
Bordetella pertussis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Bordetella pertussis ?
-
?
filamentous haemagglutinin precursor + H2O DegP contributes to degrading the filamentous haemagglutinin precursor when it is blocked intracellularly Bordetella pertussis ?
-
?

Synonyms

Synonyms Comment Organism
DegP
-
Bordetella pertussis

General Information

General Information Comment Organism
malfunction Bordetella pertussis lacking the periplasmic chaperone/protease DegP has a strong growth defect at 37°C, and the integrity of its outer membrane is compromised Bordetella pertussis
physiological function DegP is critical for growth and for membrane integrity of Bordetella pertussis at 37°C. The chaperone activity of DegP markedly alleviates the periplasmic stress, DegP chaperones the extended filamentous haemagglutinin polypeptide in the periplasm and is thus involved in the two-partner secretion pathway Bordetella pertussis