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11  structures 3401  species 1  interaction 4380  sequences 13  architectures

Family: FHIPEP (PF00771)

Summary: FHIPEP family

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This is the Wikipedia entry entitled "FHIPEP protein family". More...

FHIPEP protein family Edit Wikipedia article

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.

References

  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. PMC 206975Freely accessible. 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. 
  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. PMC 206022Freely accessible. PMID 1592799. 

This article incorporates text from the public domain Pfam and InterPro IPR001712

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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FHIPEP family Provide feedback

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001712

The Flagellar/Hr/Invasion Proteins Export Pore (FHIPEP) family [PUBMED:8253684, PUBMED:8316211] consists of a number of proteins that constitute the type III secretion (or signal peptide-independent) pathway apparatus [PUBMED:1365398, PUBMED:1592799]. 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 [PUBMED:8316211]. 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 [PUBMED:8002587]; and the secretion system apparatus protein SsaV from Salmonella typhimurium which is required for the secretion of the SpvB toxin [PUBMED:18248436].

Gene Ontology

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Domain organisation

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Alignments

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(15209)
NCBI
(22945)
Meta
(939)
RP15
(988)
RP35
(2726)
RP55
(4284)
RP75
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  Seed
(437)
Full
(4380)
Representative proteomes UniProt
(15209)
NCBI
(22945)
Meta
(939)
RP15
(988)
RP35
(2726)
RP55
(4284)
RP75
(6717)
Alignment:
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  Seed
(437)
Full
(4380)
Representative proteomes UniProt
(15209)
NCBI
(22945)
Meta
(939)
RP15
(988)
RP35
(2726)
RP55
(4284)
RP75
(6717)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_983 (release 2.1)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 437
Number in full: 4380
Average length of the domain: 623.30 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 94.40 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 29.1 29.1
Trusted cut-off 29.2 29.2
Noise cut-off 27.9 28.2
Model length: 658
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

FHIPEP

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the FHIPEP domain has been found. There are 11 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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