TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
1.S.6.1.1 | Encapsulin of 259 aas and probably no TMSs, but 4 evenly spaced short regions of moderate hydrophobicity. The protein has been described by Sutter et al. 2008. Williams et al. 2018 redesigned the pore-forming loop region in encapsulin from Thermotoga maritima, and successfully enlarged the pore diameter up to an estimated 11 Å and increased mass transport rates by 7-fold. A 2.87 Å resolution cryo-EM structure has been determined (Xiong et al. 2020). It has the viral capsid protein-HK97-fold. | Bacteria |
Thermotogota | Encapsulin of Thermotoga maritima |
1.S.6.1.2 | Encapsulin shell protein, Enc or Cfp29, of 265 aas. | Bacteria |
Actinomycetota | Enc of Mycobacterium tuberculosis |
1.S.6.1.3 | The encapsulin shell protein of 280 aas with four equidistant peaks of moderate hydrophobicity. This encapsulin nanocompartment protein is formed by 60 subunits; monomers form pentamers which assemble to form shells. There are 12 pores where the pentamers meet as well as 3-fold axis channels and dimer channels; none are larger than 3-4 Angstroms in diameter. The N-terminus of the protein is inside the shell, the C-terminus is outside (He et al. 2016). The shell component is for a type 1 encapsulin nanocompartment. It assembles into proteinaceous icosahedral shells 24 nm in diameter in the presence and absence of its ferritin cargo protein. The center of cargo-loaded nanocompartments is loaded with iron. The empty encapsulin nanocompartment sequesters about 2200 Fe ions while the cargo-loaded nanocompartment can maximally sequester about 4150 Fe ions. It does not have detectable ferroxidase activity (He et al. 2016). | Bacteria |
Pseudomonadota | Encapsulin of Rhodospirillum rubrum |