TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
1.C.67.1.1 | The pore-forming hemolysin, SphH | Bacteria |
Spirochaetota | SphH of Leptospira interrogans (AAB68647) |
1.C.67.1.2 | Uncharacterized protein of 380 aas homologous to pyrophosphatases such as sphingomyelinases. | Eukaryota |
Evosea | UP of Entamoeba histolytica |
1.C.67.1.3 | Phospholipase C, Hlb, of 330 aas. Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. It has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine. S. aureus β-hemolysin impairs oxygen transport without causing hemolysis. A novel role for Hlb as a sphingomyelinase in impairing RBC function under non-lytic conditions, sheds light on the mechanism behind hypoxia associated with S. aureus infection (Li et al. 2025). | None |
Bacillati, Bacillota | Hlb of Staphylococcus aureus |