D0LZ73 · FER_HALO1
- ProteinEncapsulated ferritin-like protein
- Genefer
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids131 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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
- 4 Fe2+ + O2 + 4 H+ = 4 Fe3+ + 2 H2OThis reaction proceeds in the forward direction.
Activity regulation
The ferroxidase activity is inhibited by zinc.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 30 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 30 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 60 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 60 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 63 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 63 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | encapsulin nanocompartment | |
Molecular Function | ferroxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | iron ion transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEncapsulated ferritin-like protein
- EC number
- Short namesEncFtn
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Myxococcota > Polyangia > Haliangiales > Kofleriaceae > Haliangium
Accessions
- Primary accessionD0LZ73
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458833 | 1-131 | Encapsulated ferritin-like protein | |||
Sequence: MSSEQLHEPAELLSEETKNMHRALVTLIEELEAVDWYQQRADACSEPGLHDVLIHNKNEEVEHAMMTLEWIRRRSPVFDAHMRTYLFTERPILELEEEDTGSSSSVAASPTSAPSHGSLGIGSLRQEGKED |
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).
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
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 96-131 | Disordered | ||||
Sequence: EEEDTGSSSSVAASPTSAPSHGSLGIGSLRQEGKED | ||||||
Compositional bias | 98-119 | Polar residues | ||||
Sequence: EDTGSSSSVAASPTSAPSHGSL | ||||||
Region | 98-131 | Targeting peptide | ||||
Sequence: EDTGSSSSVAASPTSAPSHGSLGIGSLRQEGKED |
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
Belongs to the ferritin-like superfamily. EncFtn family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length131
- Mass (Da)14,799
- Last updated2009-12-15 v1
- ChecksumA4D1423741B42FA0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 98-119 | Polar residues | ||||
Sequence: EDTGSSSSVAASPTSAPSHGSL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001804 EMBL· GenBank· DDBJ | ACY16335.1 EMBL· GenBank· DDBJ | Genomic DNA |