9.B.233.  The Mitosomal β-Barrel Outer Membrane Protein of 30 kDa (MBOMP30) Family

Entamoeba possess a highly divergent mitochondrion-related organelle known as the mitosome. Santos et al. 2015 described the Mitosomal β-barrel Outer Membrane Protein of 30 kDa (MBOMP30). MBOMP30 has a predominant β-sheet structure with 8 or 10 predicted β-strands. Localization to Entamoeba histolytica mitosomal outer membranes was demonstrated. The deletion of the putative C-terminal β-signal, a sequence believed to guide β-barrel outer membrane protein (BOMP) assembly, did not affect membrane integration but abolished the formation of a ~240 kDa complex. MBOMP30 represents the seventh subclass of eukaryotic BOMPs discovered as of 2015 and lacks detectable homologs outside Entamoeba.


 

References:

Santos, H.J., K. Imai, T. Makiuchi, K. Tomii, P. Horton, A. Nozawa, M. Ibrahim, Y. Tozawa, and T. Nozaki. (2015). A novel Mitosomal β-barrel Outer Membrane Protein in Entamoeba. Sci Rep 5: 8545.

Examples:

TC#NameOrganismal TypeExample
9.B.233.1.1

The mitosomal outer membrane β-barrel protein of 8 or 10 β-strands, MBOMP30, of 288 aas with no N-terminal targetting sequence (Santos et al. 2015).

MBOMP30 of Entamoeba histolytica