They are highly versatile systems and protect cargo proteins from environmental damage and optimize the efficiency of enzymatic processes.

[3] The encapsulin systems were first identified through the use of bioinformatics that linked capsid-like proteins to specific operons in bacterial and archaeal genomes.

[4] When protein nanocompartments were discovered in 1994, and later renamed encapsulins, they were found in the supernatant fluid of the Brevibacterium linens culture.

[6] In 2008, encapsulins were identified as protein-based systems for compartmentalization, serving specific functions within cellular organisms.

Recent advances in metagenomics, cryo-electron microscopy, and X-ray crystallography have expanded the known diversity and revealed more intricate details about the assembly and functionality of encapsulins.

Encapsulin shells compromise icosahedral complexes (12 vertices, 20 faces, 30 edges) formed as a result of self-assembly of protomers.

For example: Encapsulins serve many physiological functions, including catalysis of specialized reactions involving reactive species, iron detoxification and mineral storage, response to oxidative stress, and secondary metabolism.

They belong to the Pfam family (Encapsulating Protein for Peroxidase) and use short C-terminal targeting (TPs) for cargo loading.

This family of encapsulins provide a controlled environment for iron storage and detoxification, as well as preventing oxidative stress.

They are usually associated with various cargo enzymes like cysteine desulfurase, polyprenyl transferase, terpene cyclase, and xylulose kinase.

[9] They have a truncated form of the HK97-fold and are considered putative, with their ability to self-assemble and encapsulate cargo proteins still unknown.

In synthetic biology, research is focusing on engineering encapsulin systems to perform novel tasks, like drug synthesis or bioremediation.