Summary: Extended Signal Peptide of Type V secretion system
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Extended Signal Peptide of Type V secretion system Provide feedback
This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N-terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). So far, the ESPR is present only in Gram-negative bacterial proteins originating from the classes Beta- and Gamma-proteobacteria. ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation. Deletion of ESPR causes mis-folding of the TAAs passenger domain in the periplasm , substantially impairing its translocation across the outer membrane [3].
Literature references
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Desvaux M, Cooper LM, Filenko NA, Scott-Tucker A, Turner SM, Cole JA, Henderson IR;, FEMS Microbiol Lett. 2006;264:22-30.: The unusual extended signal peptide region of the type V secretion system is phylogenetically restricted. PUBMED:17020545 EPMC:17020545
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Desvaux M, Scott-Tucker A, Turner SM, Cooper LM, Huber D, Nataro JP, Henderson IR;, Microbiology. 2007;153:59-70.: A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism. PUBMED:17185535 EPMC:17185535
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Leyton DL, Rossiter AE, Henderson IR;, Nat Rev Microbiol. 2012;10:213-225.: From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis. PUBMED:22337167 EPMC:22337167
External database links
| PANDIT: | PF13018 |
| Pseudofam: | PF13018 |
| SYSTERS: | ESPR |
This tab holds annotation information from the InterPro database.
InterPro entry IPR024973
The extended signal peptide region (ESPR) is a highly conserved region found at the N terminus of the signal peptides of proteins belonging to the Type V secretion systems [PUBMED:17020545, PUBMED:17185535]. These proteins include the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (T5cSS). ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (290) |
Full (2495) |
Representative proteomes | NCBI (2182) |
Meta (23) |
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| RP15 (52) |
RP35 (130) |
RP55 (207) |
RP75 (281) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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Format an alignment
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (290) |
Full (2495) |
Representative proteomes | NCBI (2182) |
Meta (23) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (52) |
RP35 (130) |
RP55 (207) |
RP75 (281) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
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.
Note: You can also download the data file for the tree.
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
| Seed source: | Desvaux M |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Coggill P, Desvaux M |
| Number in seed: | 290 |
| Number in full: | 2495 |
| Average length of the domain: | 24.40 aa |
| Average identity of full alignment: | 44 % |
| Average coverage of the sequence by the domain: | 1.62 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 24 | ||||||||||||
| Family (HMM) version: | 1 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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