Haemolysin E (HlyE); This family consists of several enterobacterial haemolysin (HlyE) ...
4-293
3.51e-145
Haemolysin E (HlyE); This family consists of several enterobacterial haemolysin (HlyE) proteins.Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. HlyE is unrelated to the well characterized pore-forming E. coli hemolysins of the RTX family, haemolysin A (HlyA), and the enterohaemolysin encoded by the plasmid borne ehxA gene of E. coli 0157. However, it is evident that expression of HlyE in the absence of the RTX toxins is sufficient to give a hemolytic phenotype in E. coli. HlyE is a protein of 34 kDa that is expressed during anaerobic growth of E. coli. Anaerobic expression is controlled by the transcription factor, FNR, such that, upon ingestion and entry into the anaerobic mammalian intestine, HlyE is produced and may then contribute to the colonization of the host.
Pssm-ID: 399246 Cd Length: 333 Bit Score: 411.53 E-value: 3.51e-145
alpha pore-forming toxin (alpha-PFT) hemolysin E (HlyE, ClyA or SheA) in Escherichia coli, ...
14-292
9.08e-103
alpha pore-forming toxin (alpha-PFT) hemolysin E (HlyE, ClyA or SheA) in Escherichia coli, Salmonella typhi, and Shigella flexneri, and similar proteins; This family of alpha pore-forming toxins (alpha-PFTs) includes hemolysin E (HlyE; also called cytolysin (ClyA) or silent hemolysin A (SheA)), produced by certain strains of Escherichia coli, as well as by Salmonella enterica and Shigella flexneri, among others. HlyE is responsible for the hemolytic activity of certain strains of E. coli, including the pathogenic strain E. coli O157. Distinct from many secreted toxins and effectors, HlyE is delivered by outer-membrane vesicles (OMVs). HlyE is unrelated to the well-characterized pore-forming E. coli hemolysins of the RTX (repeats in toxin) family, hemolysin A (HlyA), and the enterohemolysin encoded by the plasmid borne ehxA gene of E. coli 0157. However, they all have the common structural features of an elongated, entirely alpha-helical domain, except for a short hydrophobic beta-hairpin known as the beta-tongue. The HlyE is monomeric in the periplasm where it forms a disulfide bond to prevent oligomerization. In the OMVs, it oligomerizes via a sequential mechanism to form a circular dodecameric pore structure that is active. The pore structure concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. HlyE/ClyA represents a prototype of the structural ClyA family of alpha-PFT which includes toxins that share structural similarity with HlyE, and includes Bacillus cereus HblB, Aeromonas hydrophila AhlB, and Bacillus thuringiensis Cry6Aa. Expression of HlyE in the absence of the RTX toxins is sufficient to give a hemolytic phenotype in E. coli. HlyE is expressed during anaerobic growth of E. coli. Anaerobic expression is controlled by the transcription factor, FNR (regulator of fumarate and nitrate reduction), such that, upon ingestion and entry into the anaerobic mammalian intestine, HlyE is produced and may then contribute to the colonization of the host.
Pssm-ID: 439354 Cd Length: 247 Bit Score: 300.75 E-value: 9.08e-103
Haemolysin E (HlyE); This family consists of several enterobacterial haemolysin (HlyE) ...
4-293
3.51e-145
Haemolysin E (HlyE); This family consists of several enterobacterial haemolysin (HlyE) proteins.Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. HlyE is unrelated to the well characterized pore-forming E. coli hemolysins of the RTX family, haemolysin A (HlyA), and the enterohaemolysin encoded by the plasmid borne ehxA gene of E. coli 0157. However, it is evident that expression of HlyE in the absence of the RTX toxins is sufficient to give a hemolytic phenotype in E. coli. HlyE is a protein of 34 kDa that is expressed during anaerobic growth of E. coli. Anaerobic expression is controlled by the transcription factor, FNR, such that, upon ingestion and entry into the anaerobic mammalian intestine, HlyE is produced and may then contribute to the colonization of the host.
Pssm-ID: 399246 Cd Length: 333 Bit Score: 411.53 E-value: 3.51e-145
alpha pore-forming toxin (alpha-PFT) hemolysin E (HlyE, ClyA or SheA) in Escherichia coli, ...
14-292
9.08e-103
alpha pore-forming toxin (alpha-PFT) hemolysin E (HlyE, ClyA or SheA) in Escherichia coli, Salmonella typhi, and Shigella flexneri, and similar proteins; This family of alpha pore-forming toxins (alpha-PFTs) includes hemolysin E (HlyE; also called cytolysin (ClyA) or silent hemolysin A (SheA)), produced by certain strains of Escherichia coli, as well as by Salmonella enterica and Shigella flexneri, among others. HlyE is responsible for the hemolytic activity of certain strains of E. coli, including the pathogenic strain E. coli O157. Distinct from many secreted toxins and effectors, HlyE is delivered by outer-membrane vesicles (OMVs). HlyE is unrelated to the well-characterized pore-forming E. coli hemolysins of the RTX (repeats in toxin) family, hemolysin A (HlyA), and the enterohemolysin encoded by the plasmid borne ehxA gene of E. coli 0157. However, they all have the common structural features of an elongated, entirely alpha-helical domain, except for a short hydrophobic beta-hairpin known as the beta-tongue. The HlyE is monomeric in the periplasm where it forms a disulfide bond to prevent oligomerization. In the OMVs, it oligomerizes via a sequential mechanism to form a circular dodecameric pore structure that is active. The pore structure concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. HlyE/ClyA represents a prototype of the structural ClyA family of alpha-PFT which includes toxins that share structural similarity with HlyE, and includes Bacillus cereus HblB, Aeromonas hydrophila AhlB, and Bacillus thuringiensis Cry6Aa. Expression of HlyE in the absence of the RTX toxins is sufficient to give a hemolytic phenotype in E. coli. HlyE is expressed during anaerobic growth of E. coli. Anaerobic expression is controlled by the transcription factor, FNR (regulator of fumarate and nitrate reduction), such that, upon ingestion and entry into the anaerobic mammalian intestine, HlyE is produced and may then contribute to the colonization of the host.
Pssm-ID: 439354 Cd Length: 247 Bit Score: 300.75 E-value: 9.08e-103
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
(CDART).
Modify your query to search against a different database and/or use advanced search options
