TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(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