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Literature summary for 3.4.24.89 extracted from

  • Hensbergen, P.J.; Klychnikov, O.I.; Bakker, D.; Dragan, I., Kelly, M.L.; Minton, N.P.; Corver, J.; Kuijper, E.J.; Drijfhout, J.W.; van Leeuwen, H.C.
    Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831 (2015), FEBS Lett., 589, 3952-3958.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Clostridioides difficile
-
-

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q183R7
-
-
Clostridioides difficile 630 Q183R7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
collagen binding protein CD2831 + H2O
-
Clostridioides difficile PAPPNTDEPIVNP + ? the removal of the collagen binding protein CD2831 from cell surface is fully attributable to PPEP-1 activity ?
collagen binding protein CD2831 + H2O
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Clostridioides difficile 630 PAPPNTDEPIVNP + ? the removal of the collagen binding protein CD2831 from cell surface is fully attributable to PPEP-1 activity ?
additional information isoform PPEP-1 has a preference for prolines surrounding the scissile bond. It exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position Clostridioides difficile ?
-
?
additional information isoform PPEP-1 has a preference for prolines surrounding the scissile bond. It exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position Clostridioides difficile 630 ?
-
?

Synonyms

Synonyms Comment Organism
PPEP-1
-
Clostridioides difficile

General Information

General Information Comment Organism
physiological function an isoform PPEP-1 knockout strain strain has no growth defect in vitro. The knockout strain demonstrates higher affinity for collagen type I with attenuated virulence in hamsters Clostridioides difficile