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PROSITE documentation PDOC00763 |
A number of bacterial proteins seem to be involved in translocating specific proteins across the bacterial cell membrane by a distinct secretory mechanism that does not require the cleavage of a signal peptide. They are evolutionary related and belong to a family [1,2,3] that currently consists of:
These proteins have all about 700 amino-acid residues. The N-terminal half is highly conserved and seems to contain 6 to 8 transmembrane domains. The C-terminal half is less conserved and seemingly devoid of transmembrane domains. It is possible that these proteins serve as pores for the export of specific proteins. We call this family FHIPEP, which stands for Flagella/Hr/ Invasion Proteins Export Pore.
As a signature pattern, we selected the best conserved region: a highly conserved hydrophilic domain between two transmembranes regions.
Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Wei Z.-M. Beer S.V. |
Title | HrpI of Erwinia amylovora functions in secretion of harpin and is a member of a new protein family. | |
Source | J. Bacteriol. 175:7958-7967(1993). | |
PubMed ID | 8253684 |
2 | Authors | Gough C.L. Genin S. Lopes V. Boucher C.A. |
Title | Homology between the HrpO protein of Pseudomonas solanacearum and bacterial proteins implicated in a signal peptide-independent secretion mechanism. | |
Source | Mol. Gen. Genet. 239:378-392(1993). | |
PubMed ID | 8316211 |
3 | Authors | Carpenter P.B. Ordal G.W. |
Title | Bacillus subtilis FlhA: a flagellar protein related to a new family of signal-transducing receptors. | |
Source | Mol. Microbiol. 7:735-743(1993). | |
PubMed ID | 8097015 |