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ART Database

CLADE: R-S-E (ARTC000001)

FAMILY: Anthrax-tox_M (ARTF000004)

Description

Members of this family are primarily found in anthrax toxin lethal factor.

InterPro - IPR015239

Anthrax toxin is a plasmid-encoded toxin complex produced by the Gram-positive, spore-forming bacteria, Bacillus anthracis. The toxin consists of three non-toxic proteins: the protective antigen (PA), the lethal factor (LF) and the edema factor (EF) [PUBMED:14570563]. These component proteins self-assemble at the surface of host cell receptors, yielding a series of toxic complexes that can produce shock-like symptoms and death. Anthrax toxin is one of a large group of Bacillus and Clostridium exotoxins referred to as binary toxins, forming independent enzymatic (A moiety) and binding (B moiety) components. The LF and EF proteins are the enzymes (A moiety) that act on cytosolic substrates, while PA is a multi-functional protein (B moiety) that binds to cell surface receptors, mediates the assembly and internalisation of the complexes, and delivers them to the host cell endosome [PUBMED:17335404]. Once PA is attached to the host receptor [PUBMED:17381430], it must then be cleaved by a host cell surface (furin family) protease before it is able to bind EF and LF. The cleavage of the N terminus of PA enables the C-terminal fragment to self-associate into a ring-shaped heptameric complex (prepore) that can bind LF or EF competitively. The PA-LF/EF complex is then internalised by endocytosis, and delivered to the endosome, where PA forms a pore in the endosomal membrane in order to translocate LF and EF to the cytosol. LF is a Zn-dependent metalloprotease that cleaves and inactivates mitogen-activated protein (MAP) kinases, kills macrophages, and causes death of the host by inhibiting cell proliferation [PUBMED:14616089, PUBMED:11700563]. EF is a calcium-and calmodulin-dependent adenylyl cyclase that can cause edema (fluid-filled swelling) when associated with PA. EF is not toxic by itself, and is required for the survival of germinated Bacillus spores within macrophages at the early stages of infection. EF dramatically elevates the level of host intracellular cAMP, a ubiquitous messenger that integrates many processes of the cell; increases in cAMP can interfere with host intracellular signalling [PUBMED:15131111]. This entry represents the central domain found in the lethal factor protein of anthrax toxin.

Sequences
Aligned domain sequences
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Unaligned domain sequences
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Full sequences
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Structures

Name Structure Additional informations
1J7N Download structure Reference structure
1JKY Download structure Reference structure
1PWP Download structure Reference structure
1PWQ Download structure Reference structure
1PWU Download structure Reference structure
1PWV Download structure Reference structure
1PWW Download structure Reference structure
6WJJ Download structure Reference structure
6ZXJ Download structure Reference structure
6ZXK Download structure Reference structure
6ZXL Download structure Reference structure
1YQY Download structure Reference structure
4DV8 Download structure Reference structure
4PKT Download structure Reference structure
4PKV Download structure Reference structure
4XM7 Download structure Reference structure
5D1S Download structure Reference structure
4PKQ Download structure Reference structure
4PKU Download structure Reference structure
4PKW Download structure Reference structure
4WF6 Download structure Reference structure
4XM6 Download structure Reference structure
4XM8 Download structure Reference structure
4PKR Download structure Reference structure
4PKS Download structure Reference structure
5D1T Download structure Reference structure
5D1U Download structure Reference structure
1ZXV Download structure Reference structure
Literature
  • PMID: 11700563
  • Origin

    Source: Pfam 34.0, rp75 Number of sequences: 6 Average length of the domain: 118 aa HMM: Model length: 186 Clustering level: 80% Alignment: ClustalO Additional information: sequences longer than 50 amino acids