TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(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. 2008Williams 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