TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.2.1.1









ICP Cry1Aa. Cry1A (Receptors in Lepidoptera are cadherin-like proteins (Fabrick et al., 2009) but can also be ABC-type efflux pumps (Chen et al. 2018). The pore-forming mechanism has been studied by Groulx et al. (2010).  This toxin causes necrosis in Drosophila species (Obata et al. 2015).

Bacteria
Firmicutes
Cry1Aa of Bacillus thuringiensis (P0A367)
*1.C.2.1.2









Pesticide crystal protein Cry4Ba (δ-endotoxin) (1136aas). Cadherin AgCad1 is the receptor for Cry4Ba (Hua et al., 2008).  Asn183 in TMS5 is essential for oligomerizatioin of the protein in themidgut membrane of the insect, and therefore for pore formation and toxicity (Likitvivatanavong et al. 2006).

Bacteria
Firmicutes
Cry4Ba of Bacillus thuringiensis (P05519)
*1.C.2.1.3









Pesticidal pre-pore-forming crystal protein, Cry1Ab; insecticidal endotoxin (1155 aas). (90% identical to Cry1Aa; (1.C.2.1.1) Kills Manduca sexta. There are several receptors (Arenas et al., 2010).  Also called bt2, Cry1-2, Cry1A(b) and CryIC1.  Mutations affecting pre-pore oligomerization and toxin pore formation have been described (Jiménez-Juárez et al. 2007).

Bacteria
Firmicutes
Cry1Ab of Bacillus thuringiensis (P0A370)
*1.C.2.1.4









Cry1Ac (85% identical to Cry1Aa (TC#1.C.2.1.1). May use MRP-4-like ABC transporter as a receptor in Bombyx mori (Atsumi et al., 2012).

Bacteria
Firmicutes
Cry1Ac of Bacillus thuringiensis (D3XF72)
*1.C.2.1.5









Pesticidal crystal protein of 1144 aas, Cry8.

Bacteria
Firmicutes
Cry8 of Bacillus thurengiensis
*1.C.2.1.6









The Cry8Ea1 toxin of 1164 aas.  The 2.2-Å crystal structure has been reported (Guo et al. 2009). Cry8Ea1 is specifically toxic to the underground larvae of Holotrichia parallela (Jia et al. 2014).

Bacteria
Firmicutes
Cry8Ea1 of Bacillus thuringiensis
*1.C.2.1.7









Pesticidal crystal protein (ICP) Cry3Aa (Andreev et al., 2009).

Bacteria
Firmicutes
Cry3Aa of Bacillus thuringiensis (P0A380)
*1.C.2.1.8









Parasporin 1, PS1 or Cry41Aa of 825 aas (Akiba and Okumura 2016). Also called Cancer cell-killing Cry protein, parasporin-3.

Bacteria
Firmicutes
PS1 of Bacillus thuringiensis
*1.C.2.2.1









Insecticidal crystal protein, Cry11Aa of 643 aas.  Cry and Cyt toxins are both oligomeric pore-formers that act synergistically with each other via direct protein-protein interactions (López-Diaz et al. 2013). Target tissue cellular responses to the toxin have been determined (Canton et al. 2015).

Bacteria
Firmicutes
Cry11Aa of Bacillus thuringiensis
*1.C.2.2.2









Insect pore-forming toxin Cry2Ab (CryB2, CryIIA(b)) of 633 aas. Exposure of helices α4 and α5 is important for the mode of action of Cry2Ab (Xu et al. 2018). It's receptor in the insect membrane is ABCC1 (TC# 3.A.1.208.45) (Chen et al. 2018).

Bacteria
Firmicutes
CryAb of Bacillus thuringiensis
*1.C.2.3.1









Pesticidal crystal protein (ICP) Cry13Aa

Bacteria
Firmicutes
Cry13Aa of Bacillus thuringiensis (Q45755)
*1.C.2.3.2









Delta-endotoxin, Cry5B, of 1245 aas is lethal to nematodes. Active Cry5B can be expressed intracellularly in and released extracellularly from Lactococcus lactis via a holin, showing potential for future use as an anthelminthic that could be delivered orally in a food-grade microbe. (Durmaz et al. 2015). 

Bacteria
Firmicutes
Cry5B of Bacillus thuringiensis