I6WZG6 · ENCAP_MYCTU

Function

function

Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls (PubMed:24855650, PubMed:34751132).
Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo (PubMed:24855650).
Probably involved in protection against oxidative damage from the host immune response (Probable) (PubMed:34751132).
A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity (PubMed:9596740).

Miscellaneous

Stimulates a strong IFN-gamma response in memory immune C57BL/6J mouse spleen T cells, recognized by monoclonal antibody HYB 71-2.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentencapsulin nanocompartment
Cellular Componentextracellular region
Cellular Componentplasma membrane

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      enc
    • Synonyms
      cfp29
    • Ordered locus names
      Rv0798c

Organism names

Accessions

  • Primary accession
    I6WZG6
  • Secondary accessions
    • O07812

Proteomes

Organism-specific databases

Subcellular Location

Secreted
Cell membrane
; Peripheral membrane protein
Note: Encapsulin microcompartments of this protein encapsulating DyP are found in situ (PubMed:34751132).
Detected at low levels in short-term culture filtrate, the nanocompartment is very stable and may survive cell lysis, explaining its apparent secretion (Probable) (PubMed:9596740).
Detected in infected host (mouse J774 cell line) exosomes (PubMed:20662102).

Keywords

Phenotypes & Variants

Disruption phenotype

A single enc deletion survives less well after 3 days in 2.5 mM H2O2, pH 4.5 (mimics growth in the phagolysosome). A double dyp-enc deletion mutant cannot produce encapsulin nanocompartments, cells are highly sensitive to H2O2 at pH 4.5, mutants exhibit significant dysregulation of redox homeostasis, survive less well in C57BL/6 mouse-derived bone marrow cells and are more sensitive to pyrazinamide treatment in infected BALB/C mice.

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed; alternate
ChainPRO_00004553131-265Type 1 encapsulin shell protein
ChainPRO_00004553142-265Type 1 encapsulin shell protein, N-terminally processed

Post-translational modification

The initiator methionine is partially removed. When isolated from culture filtrate isoelectric focusing gives 3 bands, none of which are glycosylated.

Proteomic databases

Interaction

Subunit

Multimeric (PubMed:9596740).
The encapsulin nanocompartment is formed by 60 subunits (Probable). 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 (Probable)

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the encapsulin family. Family 1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    265
  • Mass (Da)
    28,830
  • Last updated
    2012-10-03 v1
  • Checksum
    00E7E96904D3B33A
MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict242in Ref. 1; CAA73350

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y12820
EMBL· GenBank· DDBJ
CAA73350.1
EMBL· GenBank· DDBJ
Genomic DNA
AL123456
EMBL· GenBank· DDBJ
CCP43546.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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