The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Homeodomain-like
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 23854: TCP pilus virulence regulatory protein

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Prepilin peptidase. [EC: 3.4.23.43]
Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L- methionine.
  • Many species of bacteria carry pili on their cell surfaces.
  • These are virulence determinants in pathogenic strains, and are assembled biosynthetically from type IV prepilin subunits.
  • Before assembly, the prepilin molecules require proteolytic processing, which is done by the prepilin peptidase.
  • Prepilin peptidase and its homologs play a central role not only in type IV pilus biogenesis but also in transport of macromolecules across cell membranes.
  • Although both peptide-bond hydrolysis and N-methylation are catalyzed by the same molecule, the methylation can be inhibited without affecting peptidase activity, and it is believed that the enzyme has two separate catalytic sites.
  • Belongs to peptidase family A24.
2 D2YK24 D2YK24