A1R6Q9 · PAFA_PAEAT
- ProteinPup--protein ligase
- GenepafA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids454 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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.
Miscellaneous
The reaction mechanism probably proceeds via the activation of Pup by phosphorylation of its C-terminal glutamate, which is then subject to nucleophilic attack by the substrate lysine, resulting in an isopeptide bond and the release of phosphate as a good leaving group.
Catalytic activity
Pathway
Protein degradation; proteasomal Pup-dependent pathway.
Protein modification; protein pupylation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 53 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 55 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 57 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 63 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 66 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 420 | ATP (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ligase activity, forming carbon-nitrogen bonds | |
Molecular Function | magnesium ion binding | |
Molecular Function | ubiquitin-like protein transferase activity | |
Biological Process | modification-dependent protein catabolic process | |
Biological Process | proteasomal protein catabolic process | |
Biological Process | protein pupylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePup--protein ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Paenarthrobacter
Accessions
- Primary accessionA1R6Q9
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000395892 | 1-454 | Pup--protein ligase | |||
Sequence: MDKRIFGIETEFGISYSSPDSRPLAPEEVARYLFRKVVSWGRSSNVFLTNGSRLYLDVGSHPEYATAECDDLAQLIAHDRAGELILDDLVDEAQARLAAEGFNGTVYLFKNNTDSAGNSYGSHENYLIPRRGEFSRLAEILIPFLVTRQLIAGAGKVLKTPHGATFAFSQRADHIWEGVSSATTRSRPIINTRDEPHADAEFYRRLHVIVGDSNMSETSALLKVGTVDLILRMIEAGVIMRDMRMENPIRSIREISHDLTGRALVRLANGRQLTALDIQREYLNKVTDFVATNGAHNAHVPLILDLWQRTLDAIESGDTSTIDTEVDWAIKKKLMDGYMRRHDLSLDSPRIAQLDLTYHDISRQRGIFFLLQARGQARRLVTETDVKDAVDAPPQTTRAKLRGDFVRRAQELGRDYTVDWVHLKLNDRAHQTILCKDPFRSVDERVDALLDSMG |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length454
- Mass (Da)51,202
- Last updated2007-02-06 v1
- ChecksumBF7CF961B39EC0E2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000474 EMBL· GenBank· DDBJ | ABM10015.1 EMBL· GenBank· DDBJ | Genomic DNA |