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14  structures 61  species 1  interaction 252  sequences 9  architectures

Family: Aerolysin (PF01117)

Summary: Aerolysin toxin

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This is the Wikipedia entry entitled "Aerolysin". More...

Aerolysin Edit Wikipedia article

Aerolysin
PDB 1pre EBI.jpg
proaerolysin
Identifiers
Symbol Aerolysin
Pfam PF01117
Pfam clan CL0345
InterPro IPR005830
PROSITE PDOC00247
SCOP 1pre
SUPERFAMILY 1pre
TCDB 1.C.4
OPM superfamily 35

In molecular biology, aerolysin is a cytolytic pore-forming toxin exported by Aeromonas hydrophila, a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections.[1][2] The mature toxin binds to eukaryotic cells and aggregates to form holes (approximately 3 nm in diameter) leading to the destruction of the membrane permeability barrier and osmotic lysis. The structure of proaerolysin has been determined to 2.8A resolution and shows the protoxin to adopt a novel fold.[2] Images of an aerolysin oligomer derived from electron microscopy and molecular dynamics simulations have helped to construct a model of the protein in its heptameric conformation, and to outline a mechanism by which this assembly might insert into lipid bilayers to form ion channels.[3]

References[edit]

  1. ^ Howard SP, Garland WJ, Green MJ, Buckley JT (June 1987). "Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila". J. Bacteriol. 169 (6): 2869–71. PMC 212202. PMID 3584074. 
  2. ^ a b Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D (January 1994). "Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states". Nature 367 (6460): 292–5. doi:10.1038/367292a0. PMID 7510043. 
  3. ^ Degiacomi MT, Iacovache I,Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, Dal Peraro M (August 2013). "Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism". Nature Chemical Biology 9 (6460): 623–629. doi:10.1038/nchembio.1312. PMID 23912165. 

This article incorporates text from the public domain Pfam and InterPro IPR005830

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

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Aerolysin toxin Provide feedback

This family represents the pore forming lobe of aerolysin.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR005830

This family represents the pore forming lobe of aerolysin, and the related toxins haemolysin and the leukocidin S subunit.

Aerolysin [PUBMED:3584074] is a cytolytic toxin exported by Aeromonas hydrophila, a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections [PUBMED:7510043]. The mature toxin binds to eukaryotic cells and aggregates to form holes (approximately 3 nm in diameter) leading to the destruction of the membrane permeability barrier and osmotic lysis. The structure of proaerolysin has been determined to 2.8A resolution and shows the protoxin to adopt a novel fold [PUBMED:7510043]. Images of an aerolysin oligomer derived from electron microscopy have helped to construct a model of the protein and to outline a mechanism by which it might insert into lipid bilayers to form ion channels [PUBMED:7510043].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Aerolisin_ETX (CL0345), which contains the following 2 members:

Aerolysin ETX_MTX2

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
(14)
Full
(252)
Representative proteomes NCBI
(279)
Meta
(4)
RP15
(15)
RP35
(29)
RP55
(36)
RP75
(43)
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Format an alignment

  Seed
(14)
Full
(252)
Representative proteomes NCBI
(279)
Meta
(4)
RP15
(15)
RP35
(29)
RP55
(36)
RP75
(43)
Alignment:
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Sequence:
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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
(14)
Full
(252)
Representative proteomes NCBI
(279)
Meta
(4)
RP15
(15)
RP35
(29)
RP55
(36)
RP75
(43)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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.

Pfam alignments:

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 View help on the curation process

Seed source: SCOP
Previous IDs: none
Type: Domain
Author: Finn RD, Bateman A, Griffiths-Jones SR
Number in seed: 14
Number in full: 252
Average length of the domain: 219.70 aa
Average identity of full alignment: 45 %
Average coverage of the sequence by the domain: 72.35 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.3 24.3
Trusted cut-off 24.6 24.7
Noise cut-off 23.6 24.2
Model length: 360
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Interactions

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

Aerolysin

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 Aerolysin domain has been found. There are 14 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 seqence.

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