PF00771

FHIPEP family

Pfam entry
Member databasePfam
Pfam typefamily
Short nameFHIPEP
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0100021

Description
Imported from IPR001712

The Flagellar/Hr/Invasion Proteins Export Pore (FHIPEP) family
[1, 2]
consists of a number of proteins that constitute the type III secretion (or signal peptide-independent) pathway apparatus
[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.

Characterized proteins from the FHIPEP family include: the flagellar biosynthesis protein FlhA which is required for formation of the rod structure of the flagellar apparatus
[5]
; and the secretion system apparatus protein SsaV fromSalmonella typhimuriumwhich is required for the secretion of the SpvB toxin
[6]
.

References
Imported from IPR001712

1.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

2.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

3.Secretion across the bacterial outer membrane. Wandersman C. Trends Genet. 8, 317-22, (1992). View articlePMID: 1365398

4.Determinants of extracellular protein secretion in gram-negative bacteria. Lory S. J. Bacteriol. 174, 3423-8, (1992). View articlePMID: 1592799

5.Molecular characterization of the Salmonella typhimurium flhB operon and its protein products. Minamino T, Iino T, Kutuskake K. J. Bacteriol. 176, 7630-7, (1994). View articlePMID: 8002587

6.Identification of Salmonella SPI-2 secretion system components required for SpvB-mediated cytotoxicity in macrophages and virulence in mice. Browne SH, Hasegawa P, Okamoto S, Fierer J, Guiney DG. FEMS Immunol. Med. Microbiol. 52, 194-201, (2008). View articlePMID: 18248436

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