TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.10.1.1









The alpha-PFT, Haemolysin E, HlyE or ClyA of 536 aas. A peptide derived from the putative transmembrane domain in the tail region of hemolysin E (aas 88-120) assembles in phospholipid membrane and exhibits lytic activity to human red blood cells (Yadav et al., 2009). Residues important for insertion and activity have been identified (Ludwig et al., 2010).  An unusual assembly pathway has been proposed (see family description; Fahie et al. 2013). The pore can be blocked by PAMAM dendrimers (Mandal et al. 2016).  The C-terminus directs pore formation and function (Sathyanarayana et al. 2016).  Similar in structure to Cry6Aa (TC# 1.C.41.2.1) although sequence similarity could not be discerned (Dementiev et al. 2016 and unpublished results).  The C-terminal domain is not directly involved in the pore structure, but is not a passive player in pore formation as it plays important roles in mediating the transition through intermediary steps leading to successful pore formation in a membrane (Sathyanarayana et al. 2016). Transmembrane oligomeric intermediates or "arcs" probably form stable proteolipidic complexes consisting of protein arcs with toroidal lipids lining the free edges (Desikan et al. 2017). High-resolution cryo-EM structures revealed that ClyA pore complexes can exist as oligomers of a tridecamer and a tetradecamer, at estimated resolutions of 3.2 Å and 4.3 Å, respectively. The 2.8 A cryo-EM structure of a dodecamer dramatically improves the existing structural model. Structural analysis indicates that protomers from distinct oligomers resemble each other, and neighboring protomers adopt a conserved interaction mode. A stabilized intermediate state of ClyA during the transition process from soluble monomers to pore complexes was identified. Even without the formation of mature pore complexes, ClyA can permeabilize membranes and allow leakage of particles less than ~400 Daltons. In addition, ClyA forms pore complexes in the presence of cholesterol within artificial liposomes.

Bacteria
Proteobacteria
HlyE or ClyA of E. coli
*1.C.10.1.2









Eukaryotic ClyA homologue of 322 aas.

Eukaryota
Saprolegniales
ClyA homologue of Saprolegnia diclina
*1.C.10.2.1









ClyA homologue of 316 aas

Eukaryota
Saprolegniales
ClyA homologue of Saprolegnia diclina
*1.C.10.3.1









Insect ClyA homology of 433 aas

Eukaryota
Metazoa
ClyA homologue of Nasonia vitripennis (Parasitic wasp)
*1.C.10.3.2









Insect ClyA homologue of 354 aas

Eukaryota
Metazoa
ClyA homologue of Drosophila ananassae (Fruit fly)