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cyaA bifunctional adenylate cyclase toxin/hemolysin CyaA [ Bordetella pertussis Tohama I ]

Gene ID: 2664492, discontinued on 1-Apr-2020
  • This record was discontinued.

Summary

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Gene symbol
cyaA
Gene description
bifunctional adenylate cyclase toxin/hemolysin CyaA
Locus tag
BP_RS03785
Gene type
protein coding
Organism
Bordetella pertussis Tohama I (strain: Tohama I)
Lineage
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella
Old locus tag
BP0760
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Genomic regions, transcripts, and products

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Genomic Sequence:
NC_002929.2

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Data suggest that regulation of adenylate cyclase toxin (ACT)-phospholipase A (PLA) activity as a target for therapeutic control of the disease.
    Title: Phospholipase A activity of adenylate cyclase toxin mediates translocation of its adenylate cyclase domain.
  2. Substitutions of negatively charged residues then revealed that two clusters of negative charges within the linker segment control the size and the propensity of CyaA pore formation, thereby restricting the cell-permeabilizing capacity of CyaA.
    Title: Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.
  3. Data indicate potential Zn2+-binding site in the bifunctional hemolysin-adenylate cyclase (CyaA-Hly toxin) fragment.
    Title: Zn(2+)-dependent autocatalytic activity of the Bordetella pertussis CyaA-hemolysin.
  4. We suggest that these N-glycans form a defined clustered saccharide patch that enables multivalent contact of CR3 with CyaA, enhancing both affinity and specificity of the integrin-toxin interaction.
    Title: Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding.
  5. results suggest that the loop-helix-loop motif at the C-terminal end of AC is crucial during CaM binding for stabilizing the AC catalytic loop in an active configuration.
    Title: Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studies.
  6. the calcium-dependent CyaA translocation may be driven in part by the electrical field across the membrane. This
    Title: Bordetella pertussis adenylate cyclase toxin translocation across a tethered lipid bilayer.
  7. Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.
    Title: Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.
  8. C terminal lobe of calmodulin blocks a region of domain adenyl cyclase of the CyaA to keep the geometry of the catalytic site in an activated form.
    Title: Differential role of calmodulin and calcium ions in the stabilization of the catalytic domain of adenyl cyclase CyaA from Bordetella pertussis.
  9. CyaA production via activation of the NALP3 inflammasome polarizes T cell responses toward the T helper type (Th)17 cell.
    Title: Inflammasome activation by adenylate cyclase toxin directs Th17 responses and protection against Bordetella pertussis.
  10. both edema factor and CyaA have a rather broad substrate specificity and exhibit cytidylyl and uridylyl cyclase activity. Both cCMP and cUMP may contribute to toxin actions.
    Title: Cytidylyl and uridylyl cyclase activity of bacillus anthracis edema factor and Bordetella pertussis CyaA.
Submit: New GeneRIF Correction See all GeneRIFs (20)

General protein information

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Preferred Names
bifunctional adenylate cyclase toxin/hemolysin CyaA

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_002929.2 Reference assembly

    Range
    776228..781348
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. WP_010929995.1 bifunctional adenylate cyclase toxin/hemolysin CyaA [Bordetella pertussis]

    See identical proteins and their annotated locations for WP_010929995.1

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P0DKX7.1

Gene LinkOut

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Research Materials