A0A8T6RKY2 · A0A8T6RKY2_9ARCH

Function

function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Cleavage of peptide bonds with very broad specificity.
    EC:3.4.25.1 (UniProtKB | ENZYME | Rhea)

Activity regulation

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site2Nucleophile

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentproteasome core complex, beta-subunit complex
Molecular Functionthreonine-type endopeptidase activity
Biological Processproteasomal protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Proteasome subunit beta
  • EC number
  • Alternative names
    • 20S proteasome beta subunit
    • Proteasome core protein PsmB

Gene names

    • Name
      psmB
    • ORF names
      EAX96_16135

Organism names

Accessions

  • Primary accession
    A0A8T6RKY2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for propeptide, chain.

TypeIDPosition(s)Description
PropeptidePRO_50359780721Removed in mature form; by autocatalysis
ChainPRO_50359780712-207Proteasome subunit beta

Keywords

Interaction

Subunit

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.

Family & Domains

Sequence similarities

Belongs to the peptidase T1B family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    207
  • Mass (Da)
    22,546
  • Last updated
    2022-10-12 v1
  • Checksum
    CBE51726E4E8B783
MTTTLGIISNDGVILAADRRVSAGESFIASKQGEKIHKIDEFIGISIAGLVSDAQDLIDRLRAEFKLYKYERGYQISLSAAAQLTAKIFHSSFRQGMPLYTEIIIAGLDKEKNEPHLYVLDPSGALIPDKYFISTGSGSPVSYGVLEGNYKRDISREDAVKLAVRALNAAIERNPHTGNGIDVAIITKNGYELVSEEKINEILKGGS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RDOG01000017
EMBL· GenBank· DDBJ
NHI94019.1
EMBL· GenBank· DDBJ
Genomic DNA

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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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