| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.C.126.1.1 | Hemolysin C, HlyC or TlyC, of 268 aas. Pore formation was demonstrated by the inhibition of hemolysis with molecules of 2.0 to 2.3 nm in diameter and the release of 86rubidium from erythrocytes without hemoglobin release after exposure to native hemolysin (Hyatt and Joens 1997). | Bacteria |
Spirochaetota | HlyC of Brachyspira (Treponema, Serpulina) hyodysenteriae (Q54318) |
|
1.C.126.1.2 | Co2+-resistance protein, CorC, of 292 aas and 0 TMSs (Sponder et al. 2010). The E. coli orthologue (P6AE78) is 97% identical to the S. enterica protein. | Bacteria |
Pseudomonadota | CorC of Salmonella typhimurium (P0A2L3) |
|
1.C.126.1.3 | DUF21-CBS-HlyC domain-containing protein of286 aas and 0 TMSs. | Bacteria |
Pseudomonadota | HlyC-like protein of Francisella tularensis |
|
1.C.126.1.4 | Hemolysin of 159 aas | Bacteria |
Spirochaetota | Hemolysin of Treponema pallidum |