TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.14.1.1









Cytohemolysin precursor, HlyA (Vibrio cholerae cytolysin, VCC) is a beta-barrel pore-forming toxin (beta-PFT). A cryo-electron microscopic study revealed low resolution structures for different functional forms (Dutta et al., 2009). Crystal structures of the soluble and transmembrane heptamer reveal common features among disparate pore-forming toxins (De and Olson, 2011). The toxin forms transmembrane heptameric β-barrel channels with two lectin activities on the β-prism and the β-trefoil (Rai et al. 2013).  A ring of tryptophan residues forms the narrowest constriction in the transmembrane channel reminiscent of the phenylalanine clamp identified in anthrax protective antigen (Krantz et al., 2005).  A single point mutation prevents membrane integration and pore formation (Paul and Chattopadhyay 2012).  The deletion of the pre-stem segment does not affect membrane binding and pre-pore oligomer formation, but it critically abrogates the functional pore-forming activity of VCC (Paul and Chattopadhyay 2013).  The membrane-bound monomer can not form pores (Rai and Chattopadhyay 2014).  VCC can be delivered to host cells via extracellular bacterial vesicles (Elluri et al. 2014).  Loops within the membrane-proximal region of VCC play critical roles in determining the functional interactions of the toxin with the membrane lipids that allow pore formation (Rai and Chattopadhyay 2015).  VCC may interfer with signalling in the target cell as well as form pores (Khilwani and Chattopadhyay 2015).  A functional map of the VCC membrane-binding surface has been published (De et al. 2015).  Residues involved in oligomerization have been identified (Rai and Chattopadhyay 2016).

Bacteria
Proteobacteria
HlyA (VCC) precursor of Vibrio cholerae
*1.C.14.1.2









Cytohemolysin 1 precursor, Hly1
Bacteria
Proteobacteria
Hly1 of Aeromonas hydrophila
*1.C.14.1.3









Vibrio vulnificus hemolysin (VVH-A).  Consists of three domains:  Hemolysin N (residues 1 - 200), Leukocidin (residues 220 - 480) and Ricin (690 - 600).

Bacteria
Proteobacteria
VVH-A of Vibrio vulnificus (P19247)
*1.C.14.1.4









β-barrel-forming Cytotoxin of 663 aas.

Bacteria
Proteobacteria
Toxin of Algicola sagamiensis
*1.C.14.1.5









β-barrel pore-forming Toxin of 612 aas

Bacteria
Proteobacteria
Toxin of Thalassomonas viridans
*1.C.14.1.6









β-barrel pore-forming toxin of 597 aas

Bacteria
Proteobacteria
Toxin of Pseudomonas mediterranea
*1.C.14.1.7









Phobalysin (Cytolysin; Hemolysin; HlyA, PhlyP ("photobacterial lysin encoded on a plasmid") of 603 aas.  48% identical to The Vibrio cholerae hemolysin (1.C.14.1.1). Forms small β-barrel pores in eukaryotic membranes causing efflux of K+ and ATP but not proteins and entry of Ca2+ and dyes (Rivas et al. 2015; von Hoven et al. 2017).

Bacteria
Proteobacteria
Phobalysin of Photobacterium damselae (Listonella damsela)