IPR042194
FHIPEP, domain 1
InterPro entry
Short name | FHIPEP_1 |
Overlapping entries |
Description
The Flagellar/Hr/Invasion Proteins Export Pore (FHIPEP) family
[3, 1] consists of a number of proteins that constitute the type III secretion (or signal peptide-independent) pathway apparatus
[2, 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.
This superfamily represents the domain 1 found in FHIPEP protein.
References
1.Homology between the HrpO protein of Pseudomonas solanacearum and bacterial proteins implicated in a signal peptide-independent secretion mechanism. Gough CL, Genin S, Lopes V, Boucher CA. Mol. Gen. Genet. 239, 378-92, (1993). View articlePMID: 8316211
2.Secretion across the bacterial outer membrane. Wandersman C. Trends Genet. 8, 317-22, (1992). View articlePMID: 1365398
3.HrpI of Erwinia amylovora functions in secretion of harpin and is a member of a new protein family. Wei ZM, Beer SV. J. Bacteriol. 175, 7958-67, (1993). View articlePMID: 8253684
4.Determinants of extracellular protein secretion in gram-negative bacteria. Lory S. J. Bacteriol. 174, 3423-8, (1992). View articlePMID: 1592799
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.40.30.60
Representative structure
3lw9: Structure of a Cytoplasmic Domain of Salmonella InvA