Recombinant E. coli fimC protein (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

FimC also known as the chaperone protein plays an essential role in the assembly of type 1 pili in Escherichia coli. Type 1 pili are hair-like appendages that mediate adhesion to host cells. FimC has a molecular weight of approximately 30 kDa. This protein is expressed in the periplasmic space of E. coli. It specifically helps in the proper folding and transport of pilus subunits including FimH to the outer membrane where the pili assemble.

Biological function summary

FimC functions as part of the chaperone-usher pathway complex an important system in pilus biogenesis. This pathway involves multiple proteins where FimC binds with pilus subunits preventing premature folding and aggregation. The interaction between FimC and pilus subunits is highly specific and facilitates the orderly assembly of the pili. FimC aids in correctly presenting these subunits to the usher protein FimD which forms the channel through which pilus components are transported to the cell surface.

Pathways

FimC connects to the bacterial adhesion pathway an important event for bacterial colonization and infection. In addition FimC plays a role in the biofilm formation pathway where it indirectly affects the structural integrity and functionality of biofilms. The FimH protein part of the same pilus assembly associates with FimC in these pathways indicating its strong connection to adhesive functions important for bacterial pathogenicity.

FimC is implicated in urinary tract infections where E. coli use type 1 pili to adhere to urinary epithelial cells. Proper functioning of FimC is critical in these infections as it supports the assembly of pili that help bacteria resist flushing by urine. Additionally the protein links to certain gastrointestinal infections caused by E. coli adhesion in the intestine. In these conditions FimC and its interaction with the chaperone FimD contribute significantly to the adhesion capabilities of the pathogens highlighting its importance in bacterial virulence.