Pili assembly chaperone, C-terminal (IPR016148)

Short name: Pili_assmbl_chaperone_C

Overlapping homologous superfamilies

Domain relationships



Most Gram-negative bacteria possess a supramolecular structure - the pili - on their surface, which mediates attachment to specific receptors. Many interactive subunits are required to assemble pili, but their assembly only takes place after translocation across the cytoplasmic membrane. Periplasmic chaperones assist pili assembly by binding to the subunits, thereby preventing premature aggregation [PMID: 8670884, PMID: 1683764]. Pili chaperones are structurally, and possibly evolutionarily, related to the immunoglobulin superfamily [PMID: 1348692, PMID: 17082819]: they contain two globular domains, with a topology identical to an immunoglobulin fold.

This entry represents the C-terminal domain of pili assembly chaperone PapD, and has a beta-sandwich fold consisting of eight strands in two sheets with a Greek key topology.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.