A0A5P9QAN6 · A0A5P9QAN6_9MICO

Function

function

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

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 ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger 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.

Pathway

Protein degradation; proteasomal Pup-dependent pathway.

Features

Showing features for active site.

131020406080100120140160180200220240260280300
TypeIDPosition(s)Description
Active site51Nucleophile

GO annotations

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

Gene names

    • Name
      psmB
    • Synonyms
      prcB
    • ORF names
      KDY119_01690

Organism names

Accessions

  • Primary accession
    A0A5P9QAN6

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for propeptide, chain.

TypeIDPosition(s)Description
PropeptidePRO_50290743891-50Removed in mature form; by autocatalysis
ChainPRO_502907439051-310Proteasome 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 by the proteasome-associated ATPase, ARC.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region267-310Disordered
Compositional bias291-310Basic and acidic residues

Sequence similarities

Belongs to the peptidase T1B family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    310
  • Mass (Da)
    32,609
  • Last updated
    2020-04-22 v1
  • Checksum
    A3342CA7393F65FB
MTPEADARLPRAFTTPGSASFVEFLAAHDPGLLPAGRVLPAGDAPAAPHGTTIVAVTYDGGVVMAGDRRATAGAMIASREIEKVFPADEYAAVGIAGSAGLALELVRLYQLELEHYEKIEGSLLSLDGKANRLSTMIRSNLGLAMQGLAVVPLFAGYDLDRDAGRIFSYDVTGGRYEEHDHHSVGSGSVFARGALKKLWRPGLDAAGAVHVAVEALYDAADDDSATGGPDPVRRIWPVVATVDAEGYRRVGDDELAALAAEIVAERTAANDARRGVRRTSASNPSDEPRPVPPEELTERTRGADSEGDTP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias291-310Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP045529
EMBL· GenBank· DDBJ
QFU98180.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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