FHIPEP protein family
From Wikipedia, the free encyclopedia
| FHIPEP | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | FHIPEP | ||||||||
| Pfam | PF00771 | ||||||||
| InterPro | IPR001712 | ||||||||
| PROSITE | PDOC00763 | ||||||||
| TCDB | 3.A.6 | ||||||||
| |||||||||
In molecular biology, the FHIPEP protein family (Flagellar/Hr/Invasion Proteins Export Pore family) consists of a number of proteins that constitute the type III secretion (or signal peptide-independent) pathway apparatus.[1][2][3][4] This mechanism translocates proteins lacking an N-terminal signal peptide across the cell membrane in one step, as it does not require an intermediate periplasmic process to cleave the signal peptide. It is a common pathway amongst Gram-negative bacteria for secreting toxic and flagellar proteins.
The pathway apparatus comprises three components: two within the inner membrane and one within the outer.[2] An FHIPEP protein is located within the inner membrane, although it is unknown which component it constitutes. FHIPEP proteins have all about 700 amino acid residues. Within the sequence, the N terminus is highly conserved and hydrophobic, suggesting that this terminus is embedded within the membrane, with 6-8 transmembrane (TM) domains, while the C terminus is less conserved and appears to be devoid of TM regions. It is possible that members of the FHIPEP family serve as pores for the export of specific proteins.