Summary: Thiol-activated cytolysin
This is the Wikipedia entry entitled "Thiol-activated cytolysin". More...
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Thiol-activated cytolysin Edit Wikipedia article
Cholesterol-binding cytolysin, previously incorrectly known as 'thiol-activated' cytolysins " are toxins produced by a variety of Gram-positive bacteria and are characterised by their ability to lyse cholesterol-containing membranes, their reversible inactivation by oxidation and their capacity to bind to cholesterol.
- Geoffroy C, Mengaud J, Cossart P, Alouf JE (1990). "Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine". J. Bacteriol. 172 (12): 7301–7305. PMC 210863. PMID 2254290.
- Geoffroy C, Alouf JE (1984). pp. 165–171. Missing or empty
- Bacterial Disease Mechanisms: Michael Wilson, Rod McNab, Brian Henderson (2002)
Thiol-activated cytolysin Provide feedback
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Internal database links
|SCOOP:||Effector_1 BRK DUF4287 CLAMP ZirS_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001869Thiol-activated cytolysins [PUBMED:2254290] are toxins produced by a variety of Gram-positive bacteria and are characterised by their ability to lyse cholesterol-containing membranes, their reversible inactivation by oxidation and their capacity to bind to cholesterol. All these proteins contain a single cysteine residue, located in their C-terminal section, which has been shown [PUBMED:2888650] to be essential for the binding to cholesterol.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||cholesterol binding (GO:0015485)|
|Biological process||pathogenesis (GO:0009405)|
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||16|
|Number in full:||1814|
|Average length of the domain:||350.20 aa|
|Average identity of full alignment:||40 %|
|Average coverage of the sequence by the domain:||84.27 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Thiol_cytolysin domain has been found. There are 16 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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