FHIPEP protein family

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FHIPEP
Identifiers
SymbolFHIPEP
PfamPF00771
InterProIPR001712
PROSITEPDOC00763
TCDB3.A.6
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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.

References[edit]

  1. ^ Wei ZM, Beer SV (December 1993). "HrpI of Erwinia amylovora functions in secretion of harpin and is a member of a new protein family". J. Bacteriol. 175 (24): 7958–67. doi:10.1128/jb.175.24.7958-7967.1993. PMC 206975. PMID 8253684.
  2. ^ a b Gough CL, Genin S, Lopes V, Boucher CA (June 1993). "Homology between the HrpO protein of Pseudomonas solanacearum and bacterial proteins implicated in a signal peptide-independent secretion mechanism". Mol. Gen. Genet. 239 (3): 378–92. doi:10.1007/bf00276936. PMID 8316211. S2CID 28775466.
  3. ^ Wandersman C (September 1992). "Secretion across the bacterial outer membrane". Trends Genet. 8 (9): 317–22. doi:10.1016/0168-9525(92)90264-5. PMID 1365398.
  4. ^ Lory S (June 1992). "Determinants of extracellular protein secretion in gram-negative bacteria". J. Bacteriol. 174 (11): 3423–8. doi:10.1128/jb.174.11.3423-3428.1992. PMC 206022. PMID 1592799.
This article incorporates text from the public domain Pfam and InterPro: IPR001712