D0LZ73 · FER_HALO1

Function

function

Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like ferroxidase that converts Fe2+ to Fe3+ iron inside the encapsulin nanocompartment (PubMed:30837306, PubMed:35080974).
Mineralized Fe3+ is released to the exterior of the decameric complex for deposition in the encapsulin nanocompartment. In solution the decamer binds 10-15 iron cations; in the encapsulin nanocompartment the decamer can bind up to 48 ions, perhaps via its internal channel, and on its exterior. The cargo-loaded nanocompartment maximally sequesters up to 4150 Fe ions (By similarity).

Catalytic activity

Activity regulation

The ferroxidase activity is inhibited by zinc.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site30Fe cation 1 (UniProtKB | ChEBI)
Binding site30Fe cation 2 (UniProtKB | ChEBI)
Binding site60Fe cation 1 (UniProtKB | ChEBI)
Binding site60Fe cation 2 (UniProtKB | ChEBI)
Binding site63Fe cation 1 (UniProtKB | ChEBI)
Binding site63Fe cation 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentencapsulin nanocompartment
Molecular Functionferroxidase activity
Molecular Functionmetal ion binding
Biological Processintracellular iron ion homeostasis
Biological Processiron ion transport

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 1.S.7.1.4the bacterial/archaeal nanocompartment encapsulin shell protein2 (banc-sp2) family

Names & Taxonomy

Protein names

  • Recommended name
    Encapsulated ferritin-like protein
  • EC number
  • Short names
    EncFtn

Gene names

    • Name
      fer
    • Ordered locus names
      Hoch_3836

Organism names

Accessions

  • Primary accession
    D0LZ73

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004588331-131Encapsulated ferritin-like protein

Interaction

Subunit

Forms dimers at all pH tested; under acidic conditions formes decamers. The N-terminal domain (residues 1-97) crystallizes as a decameric ring (PubMed:30837306).
Four decamers are loaded in the encapsulin nanocompartment in a tetrahedral arrangement. A 3 nm gap is consistently seen between the shell and the cargo. The target peptide extends away from the decameric ring, to allow binding to the interior of the encapsulin nanocompartment shell (PubMed:35080974).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region96-131Disordered
Compositional bias98-119Polar residues
Region98-131Targeting peptide

Domain

The decamer has negatively charged patches on its exterior, and a negatively charged tunnel at the center, the charges are probably metal-binding sites.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    131
  • Mass (Da)
    14,799
  • Last updated
    2009-12-15 v1
  • Checksum
    A4D1423741B42FA0
MSSEQLHEPAELLSEETKNMHRALVTLIEELEAVDWYQQRADACSEPGLHDVLIHNKNEEVEHAMMTLEWIRRRSPVFDAHMRTYLFTERPILELEEEDTGSSSSVAASPTSAPSHGSLGIGSLRQEGKED

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias98-119Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001804
EMBL· GenBank· DDBJ
ACY16335.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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