Proteasome-associated ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Proteasome endopeptidase complex, beta component Threonine peptidase. MEROPS family T01B; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.

Protein of unknown function.

Prokaryotic ubiquitin-like protein Pup; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Belongs to the prokaryotic ubiquitin-like protein family.

Proteasome accessory factor A; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine.

Proteasome accessory factor A.

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif.

Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family.