TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.41.1.1









The tripartite haemolysin BL (Sastalla et al. 2013).

Bacteria
Firmicutes
HBL of Bacillus cereus
*1.C.41.1.2









Haemolysin YhlA
Bacteria
Proteobacteria
YhlA of Edwardsiella tarda
*1.C.41.1.3









The non-hemolytic pore-forming cyto-enterotoxin, Nhe (Fagerlund et al., 2008; Sastalla et al. 2013), a three-partite toxin.  Pore formation and subsequent lysis of target cells caused by Nhe is an orchestrated process comprising three steps: (i) formation of NheB/C oligomers in solution, (ii) attachment of the oligomers to the cell membrane, (iii) binding of NheA to the oligomers. The benefit of these complexes is more stable cell binding as well as stronger and earlier cytotoxic effects. High molecular mass hetero-oligomers (~620 kDa), probably consist of one NheC and up to 15 NheB. NheBC induces membrane permeability. Formation of stable transmembrane channels with a conductance of about 870 pS and a diameter of about 2 nm due to the application of NheBC could be demonstrated in lipid bilayer experiments (Zhu et al. 2015). Thus, the NheBC complex increases the membrane permeability prior to the emergence of full pores containing also NheA.  Can induce apoptosis (Sastalla et al. 2013), a three-partite toxin.  Pore formation and subsequent lysis of target cells caused by Nhe is an orchestrated process comprising three steps: (i) formation of NheB/C oligomers in solution, (ii) attachment of the oligomers to the cell membrane, (iii) binding of NheA to the oligomers. The benefit of these complexes is more stable cell binding as well as stronger and earlier cytotoxic effects. High molecular mass hetero-oligomers (~620 kDa), probably consist of one NheC and up to 15 NheB. NheBC induces membrane permeability. Formation of stable transmembrane channels with a conductance of about 870 pS and a diameter of about 2 nm due to the application of NheBC could be demonstrated in lipid bilayer experiments (Zhu et al. 2015). Thus, the NheBC complex increases the membrane permeability prior to the emergence of full pores containing also NheA.  Can induce apoptosis (Liu et al. 2016).

Bacteria
Firmicutes
Nhe of Baccilus cereus
Nhe-L1 (NheB; 402aas) (Q63CS3)
Nhe-L2 (NheA; 386aas) (Q63CS4)
NheC (359aas) (Q2TM55)
*1.C.41.2.1









Nematicidal pesticide pore-forming crystal protein α-toxin, Cry6Aa (Cry6A; CryVIa) of 475 aas.  It is structurally similar to HlyE (TC# 1.C.10.1.1) (Dementiev et al. 2016).  The X-ray struction of residues 1 - 396 at 1.9 Å resolution shows a structure similar to to those of Cly toxins (Huang et al. 2016).

Bacteria
Firmicutes
Cry6Aa of Bacillus thuringiensis
*1.C.41.2.2









Uncharacterized toxin of 407 aas,

Bacteria
Proteobacteria
Toxin of Pseudoalteromonas piscicida
*1.C.41.2.3









Uncharacterized toxin of 383 aas.

Bacteria
Firmicutes
Toxin of Clostridium kluyveri
*1.C.41.2.4









Uncharacterized toxin of 389 aas

Eukaryota
Fungi
Toxin of Schizophyllum commune
*1.C.41.2.5









Uncharacterized toxin of 420 aas

Toxin of Hypocrea virens (Gliocladium virens) (Trichoderma virens)
*1.C.41.2.6









Putative toxin of 415 aas and 1 TMS

Bacteria
Proteobacteria
Toxin of Pseudomonas cichorii