EC Number   |
General Information |
Reference  |
|---|
   6.3.1.19 | metabolism |
proteasome-containing bacteria possess a tagging system that directs proteins to proteasomal degradation by conjugating them to a prokaryotic ubiquitin-like protein (Pup). A single ligating enzyme, PafA, is responsible for Pup conjugation to lysine side chains of protein substrates. As Pup is recognized by the regulatory subunit of the proteasome, Pup functions as a degradation tag. Ligating enzyme PafA and the proteasome can function as a modular machine for the tagging and degradation of cytoplasmic proteins |
-, 729245 |
| 6.3.1.19 | malfunction |
in a pafA knockout strain pupylated proteins are undetectable and proteasomal substrate proteins accumulate |
-, 729308 |
| 6.3.1.19 | physiological function |
pupylation is a signal for proteasomal degradation in bacteria. The prokaryotic, ubiquitin-like protein (Pup) is conjugated through its C-terminal residue to lysine side chains of substrates via an isopeptide bond |
-, 729308 |
| 6.3.1.19 | metabolism |
prokaryotic ubiquitin-like protein (Pup) is a post-translational modifier that attaches to more than 50 proteins in Mycobacteria. Proteasome accessory factor A (PafA) is responsible for Pup conjugation to substrates |
-, 729641 |
| 6.3.1.19 | metabolism |
pupylation is a bacterial post-translational modification of target proteins on lysine residues with prokaryotic ubiquitinlike protein (Pup). Pup-tagged substrates are recognized by a proteasome-interacting ATPase (Mpa) in Mycobacterium tuberculosis. Mpa unfolds pupylated substrates and threads them into the proteasome core particle for degradation |
-, 730004 |
| 6.3.1.19 | physiological function |
in Mycobacterium tuberculosis Pup tagging is important for virulence |
-, 730010 |
| 6.3.1.19 | metabolism |
pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination |
-, 730443 |
| 6.3.1.19 | physiological function |
prokaryotic ubiquitin-like protein, Pup, is conjugated to proteins by PafA, the only Pup ligase identified thus far, through the formation of an iso-peptide bond between the gamma-carboxylate of a glutamate side chain at the C terminus of Pup and the epsilon-amine of a lysine residue on the target protein. Pupylation is a cytoplasmic signal for proteasomal degradation. Pup ligase PafA conjugates the small protein Pup to lysine side chains of target proteins. Mono-Pup moieties are almost exclusively observed in vivo and are sufficient as degradation tags |
-, 744878 |
| 6.3.1.19 | physiological function |
pupylation, the bacterial equivalent of ubiquitylation, involves the conjugation of a prokaryotic ubiquitin-like protein (Pup) to protein targets. In contrast to the ubiquitin system, where many ubiquitin ligases exist, a single bacterial ligase, PafA, catalyzes the conjugation of Pup to a wide array of protein targets |
-, 745553 |
| 6.3.1.19 | evolution |
the Pup-proteasome system (PPS) is functionally related to the eukaryotic Ub-proteasome system, but the number of the involved players is smaller, comparison of reaction mechanisms, overview |
-, 745555 |
