A0A0H3D6M1 · A0A0H3D6M1_AMYMU

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.

128420406080100120140160180200220240260280
TypeIDPosition(s)Description
Active site54Nucleophile

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
    • Ordered locus names
      AMED_4894

Organism names

Accessions

  • Primary accession
    A0A0H3D6M1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for propeptide, chain.

TypeIDPosition(s)Description
PropeptidePRO_50050311121-53Removed in mature form; by autocatalysis
ChainPRO_502338939154-284Proteasome 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

Sequence similarities

Belongs to the peptidase T1B family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    284
  • Mass (Da)
    29,581
  • Last updated
    2015-09-16 v1
  • Checksum
    3CB1A30DA5B10B49
MDNTRGISGPALPAAYFSSATSSFSDFLRVQAPELLPERRVSPGAAELGIPHGTTIVACTFASGVLIAGDRRATSGNLIASRDIEKVHVTDEYSAVGIAGTAGLAVEMVRLYAVELAHYEKIEGVSLSLDGKTNKLAGMVKANLEMAMAGLAAIPLFVGYDLEAEDAKHAGRIVSYDAAGGRYEENGGYAGIGSGSLFAKSALKKLHDPDADVEGAVRVAVEALYDAADDDTASGGPDLVRRIFPSVVTITAERGAVQLSESETAAVAEAVVAGRIERQQRRLS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002000
EMBL· GenBank· DDBJ
ADJ46660.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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