TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.57.1.1









Cytotoxin B, TcdB. The minimal pore-forming region is within amino acid residues 830 and 990 including glutamate-970 and glutamate-976. These two residues are essential for pore formation (Genisyuerek et al., 2011).  Other residues important for toxicity have been identified (Zhang et al. 2014).  Residues in the translocation domain of TcdB that form the pore and function in toxin translocation have been identified (Hamza et al. 2016).

Bacteria
Firmicutes
Cytotoxin B (TcdB) of Clostridium difficile
*1.C.57.1.2









Cytotoxin A
Bacteria
Firmicutes
Cytotoxin A of Clostridium difficile
*1.C.57.1.3









Lethal toxin
Bacteria
Firmicutes
Lethal toxin (cytotoxin L) of Clostridium sordellii
*1.C.57.1.4









α-toxin
Bacteria
Firmicutes
α-toxin of Clostridium novyi
*1.C.57.1.5









Cytotoxin C, TpeL (Amimoto et al., 2007)
Bacteria
Firmicutes
TpeL of Clostridium difficile (A2PYQ6)
*1.C.57.1.6









MCF toxin of 2993 aas

Bacteria
Proteobacteria
MCF toxin of Photorhabdus asymbiotica subsp. asymbiotica (Xenorhabdus luminescens)
*1.C.57.2.1









Toxin B
Bacteria
Proteobacteria
Toxin B of E. coli plasmid p0157
*1.C.57.2.2









Cytotoxic adherence factor TC0437
Bacteria
Chlamydiae/Verrucomicrobia group
TC0437 of Chlamydia muridarum
*1.C.57.3.1









Pasteurella multocida toxin (PMT); dermonecrotic toxin (DMT); mitogenic toxin (ToxA) (Baldwin et al., 2004)
Bacteria
Proteobacteria
PMT of Pasteurella multocida (P17452)
*1.C.57.3.2









Cytotoxic necrotizing factor type 1, Cnf1 (Oswald et al., 1994)
Bacteria
Proteobacteria
Cnf1 of E. coli (AAN03786)
*1.C.57.3.3









Cytotoxic necrotizing factor type 2, Cnf2 (Oswald et al., 1994)
Bacteria
Proteobacteria
Cnf2 of E. coli (A55260)
*1.C.57.3.4









RTX (repeat in toxin) cytotoxin, also called the "multifunctional-autoprocessing RTX" (MARTXVv) toxin, or Vibrio vulnificus cytotoxin (VVC) exists in at least four distinct variants of rtxA1 that encode toxins with different arrangements of effector domains that arose by recombination.  VVC, in addition to being a pore-forming toxin, may be a transmembrane toxin with the ability to induce apoptosis in human vascular endothelial cells and tumor cells (Zhao et al. 2009).

Bacteria
Proteobacteria
RTX cytotoxin of Vibrio vulnificus (BAC97056)
*1.C.57.4.1









Putative toxin A of 294 aas

Bacteria
Spirochaetes
Toxin A of Brachyspira intermedia