1.S.10. The Bacterial/Archaeal Nanocompartment Encapsulin Shell Protein6 (BANC-SP5) Family
Encapsulin nanocompartment protein Rv1762c The system contributes to defense against oxidative stress in Mycobacterium tuberculosis (Lien et al. 2021). This nanocompartment contains the dye-decolorizing peroxidase DyP. It is important for the ability of Mtb to resist oxidative stress in low pH environments, including during infection of host cells and upon treatment with a clinically relevant antibiotic.
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Nanocompartment encapsulin of 262 aas and 2 quite hydrophobic peaks at residues 40 and 155. The nanocompartment contains the dye-decolorizing peroxidase DyP. This nanocompartment is important for the ability of Mtb to resist oxidative stress in low pH environments, including during infection of host cells and upon treatment with a clinically relevant antibiotic (Lien et al. 2021). Shell component of a type 2A encapsulin nanocompartment. It forms nanocompartments about 24 nm in diameter from 60 monomers, and probably encapsulates at least cysteine desulfurase (CyD, Acc # O32975) and allows passage of cysteine into its interior, probably involved in sulfur metabolism.
Encapsulin of Mycobacterium leprae
Heavy metal-binding domain-containing protein of 411 aas.
HMBD protein of Legionella longbeachae serogroup 1
Heavy metal-binding domain-containing protein of 376 aas and containing an internal duplication, in which the first half (residues 1 - 130) and the second half (residues 131 - 343) are similar in sequence.
HMBD protein of Singulisphaera acidiphila