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Literature summary for 6.3.1.19 extracted from
- Prokaryotic ubiquitin-like protein and its ligase/deligase enzymes (2017), J. Mol. Biol., 429, 3486-3499 .
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is a target for drug development in tuberculosis treatment | Mycobacterium tuberculosis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Mycobacterium tuberculosis |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Corynebacterium glutamicum |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Bifidobacterium adolescentis |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Thermobifida fusca |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Renibacterium salmoninarum |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Salinispora tropica |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Kocuria rhizophila |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Micrococcus luteus |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Acidothermus cellulolyticus |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Mycolicibacterium smegmatis |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Rhodococcus erythropolis |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Paenarthrobacter aurescens |
| gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview | Streptomyces coelicolor |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Mycobacterium tuberculosis |  |
| Mg2+ | required | Corynebacterium glutamicum | |
| Mg2+ | required | Bifidobacterium adolescentis | |
| Mg2+ | required | Thermobifida fusca | |
| Mg2+ | required | Renibacterium salmoninarum | |
| Mg2+ | required | Salinispora tropica | |
| Mg2+ | required | Kocuria rhizophila | |
| Mg2+ | required | Micrococcus luteus | |
| Mg2+ | required | Acidothermus cellulolyticus | |
| Mg2+ | required | Mycolicibacterium smegmatis | |
| Mg2+ | required | Rhodococcus erythropolis | |
| Mg2+ | required | Paenarthrobacter aurescens | |
| Mg2+ | required | Streptomyces coelicolor | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Mycobacterium tuberculosis | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Corynebacterium glutamicum | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Bifidobacterium adolescentis | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Thermobifida fusca | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Renibacterium salmoninarum | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Salinispora tropica | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Kocuria rhizophila | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Micrococcus luteus | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Acidothermus cellulolyticus | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Mycolicibacterium smegmatis | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Rhodococcus erythropolis | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Paenarthrobacter aurescens | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Streptomyces coelicolor | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Acidothermus cellulolyticus ATCC 43068 / 11B | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Mycobacterium tuberculosis ATCC 25618 / H37Rv | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Paenarthrobacter aurescens TC1 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Mycolicibacterium smegmatis ATCC 700084 / mc2155 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Rhodococcus erythropolis PR4 / NBRC 100887 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidothermus cellulolyticus | A0LU53 | - |
- |
| Acidothermus cellulolyticus ATCC 43068 / 11B | A0LU53 | - |
- |
| Bifidobacterium adolescentis | A1A0U7 | - |
- |
| Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a | A1A0U7 | - |
- |
| Corynebacterium glutamicum | Q8NQE1 | - |
- |
| Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 | Q8NQE1 | - |
- |
| Kocuria rhizophila | B2GIN9 | - |
- |
| Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201 | B2GIN9 | - |
- |
| Micrococcus luteus | C5CBV0 | i.e. Micrococcus lysodeikticus | - |
| Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230 | C5CBV0 | i.e. Micrococcus lysodeikticus | - |
| Mycobacterium tuberculosis | P9WNU7 | - |
- |
| Mycobacterium tuberculosis ATCC 25618 / H37Rv | P9WNU7 | - |
- |
| Mycolicibacterium smegmatis | A0QZ42 | - |
- |
| Mycolicibacterium smegmatis ATCC 700084 / mc2155 | A0QZ42 | - |
- |
| Paenarthrobacter aurescens | A1R6Q9 | i.e. Arthrobacter aurescens | - |
| Paenarthrobacter aurescens TC1 | A1R6Q9 | i.e. Arthrobacter aurescens | - |
| Renibacterium salmoninarum | A9WSH9 | - |
- |
| Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 | A9WSH9 | - |
- |
| Rhodococcus erythropolis | C0ZZU4 | - |
- |
| Rhodococcus erythropolis PR4 / NBRC 100887 | C0ZZU4 | - |
- |
| Salinispora tropica | A4X747 | - |
- |
| Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440 | A4X747 | - |
- |
| Streptomyces coelicolor | Q9RJ61 | - |
- |
| Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 | Q9RJ61 | - |
- |
| Thermobifida fusca | Q47NZ6 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Mycobacterium tuberculosis | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Corynebacterium glutamicum | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Bifidobacterium adolescentis | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Thermobifida fusca | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Renibacterium salmoninarum | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Salinispora tropica | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Kocuria rhizophila | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Micrococcus luteus | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Acidothermus cellulolyticus | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Mycolicibacterium smegmatis | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Rhodococcus erythropolis | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Paenarthrobacter aurescens | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition | Streptomyces coelicolor |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Mycobacterium tuberculosis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Corynebacterium glutamicum | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Bifidobacterium adolescentis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Thermobifida fusca | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Renibacterium salmoninarum | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Salinispora tropica | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Kocuria rhizophila | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Micrococcus luteus | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Acidothermus cellulolyticus | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Mycolicibacterium smegmatis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Rhodococcus erythropolis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Paenarthrobacter aurescens | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Streptomyces coelicolor | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Mycobacterium tuberculosis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Corynebacterium glutamicum | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Bifidobacterium adolescentis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Thermobifida fusca | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Renibacterium salmoninarum | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Salinispora tropica | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Kocuria rhizophila | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Micrococcus luteus | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Acidothermus cellulolyticus | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Mycolicibacterium smegmatis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Rhodococcus erythropolis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Paenarthrobacter aurescens | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Streptomyces coelicolor | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Acidothermus cellulolyticus ATCC 43068 / 11B | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Acidothermus cellulolyticus ATCC 43068 / 11B | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Mycobacterium tuberculosis ATCC 25618 / H37Rv | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Mycobacterium tuberculosis ATCC 25618 / H37Rv | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Paenarthrobacter aurescens TC1 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Paenarthrobacter aurescens TC1 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Mycolicibacterium smegmatis ATCC 700084 / mc2155 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Mycolicibacterium smegmatis ATCC 700084 / mc2155 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Rhodococcus erythropolis PR4 / NBRC 100887 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Rhodococcus erythropolis PR4 / NBRC 100887 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
| ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup variant used presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA, PupE is covalently attached to the protein via a GGL bridge, overview. The isopeptide bond to the lysine residue of the target protein occurs via the side-chain carboxylate | Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PafA | - |
Mycobacterium tuberculosis |
| PafA | - |
Corynebacterium glutamicum |
| PafA | - |
Bifidobacterium adolescentis |
| PafA | - |
Thermobifida fusca |
| PafA | - |
Renibacterium salmoninarum |
| PafA | - |
Salinispora tropica |
| PafA | - |
Kocuria rhizophila |
| PafA | - |
Micrococcus luteus |
| PafA | - |
Acidothermus cellulolyticus |
| PafA | - |
Mycolicibacterium smegmatis |
| PafA | - |
Rhodococcus erythropolis |
| PafA | - |
Paenarthrobacter aurescens |
| PafA | - |
Streptomyces coelicolor |
| Pup ligase | - |
Mycobacterium tuberculosis |
| Pup ligase | - |
Corynebacterium glutamicum |
| Pup ligase | - |
Bifidobacterium adolescentis |
| Pup ligase | - |
Thermobifida fusca |
| Pup ligase | - |
Renibacterium salmoninarum |
| Pup ligase | - |
Salinispora tropica |
| Pup ligase | - |
Kocuria rhizophila |
| Pup ligase | - |
Micrococcus luteus |
| Pup ligase | - |
Acidothermus cellulolyticus |
| Pup ligase | - |
Mycolicibacterium smegmatis |
| Pup ligase | - |
Rhodococcus erythropolis |
| Pup ligase | - |
Paenarthrobacter aurescens |
| Pup ligase | - |
Streptomyces coelicolor |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mycobacterium tuberculosis | |
| ATP | - |
Corynebacterium glutamicum | |
| ATP | - |
Bifidobacterium adolescentis | |
| ATP | - |
Thermobifida fusca | |
| ATP | - |
Renibacterium salmoninarum | |
| ATP | - |
Salinispora tropica | |
| ATP | - |
Kocuria rhizophila | |
| ATP | - |
Micrococcus luteus | |
| ATP | - |
Acidothermus cellulolyticus | |
| ATP | - |
Mycolicibacterium smegmatis | |
| ATP | - |
Rhodococcus erythropolis | |
| ATP | - |
Paenarthrobacter aurescens | |
| ATP | - |
Streptomyces coelicolor | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Corynebacterium glutamicum |
| 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 | Bifidobacterium adolescentis |
| 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 | Thermobifida fusca |
| 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 | Renibacterium salmoninarum |
| 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 | Salinispora tropica |
| 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 | Kocuria rhizophila |
| 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 | Micrococcus luteus |
| 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 | Acidothermus cellulolyticus |
| 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 | Mycolicibacterium smegmatis |
| 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 | Rhodococcus erythropolis |
| 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 | Paenarthrobacter aurescens |
| 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 | Streptomyces coelicolor |
| 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. Intrinsically disordered Pup is structurally unlike the stably folded ubiquitin | Mycobacterium tuberculosis |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. For Mycobacterium tuberculosis, pupylation and the recruitment of pupylated substrates to the proteasome support persistence inside host macrophages during pathogenesis. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Mycobacterium tuberculosis |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Corynebacterium glutamicum |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Bifidobacterium adolescentis |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Thermobifida fusca |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Renibacterium salmoninarum |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Salinispora tropica |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Kocuria rhizophila |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Micrococcus luteus |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Acidothermus cellulolyticus |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Mycolicibacterium smegmatis |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Rhodococcus erythropolis |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Paenarthrobacter aurescens |
| physiological function | prokaryotic ubiquitin-like protein (Pup) is a small protein that can be covalently attached to lysine side chains of cellular proteins by Pup ligase PafA. Pupylation serves as a recruitment tool for proteasomal degradation. Pup serves as both recognition and threading element in proteasomal degradation of pupylated substrates. The degradation substrate covalently modified with Pup is recruited to the Mpa-proteasome complex by docking to the Mpa coiled-coil domain, which triggers Pup to undergo a disorder-to-order transition, forming an extended helix that associates into a shared three-stranded coil with the Mpa N-terminal coiled-coil domains. The disordered N-terminal region of Pup points into the Mpa central pore, where it is engaged by the ATPase-driven pore loops for unfolding and directional translocation into the proteasome core for degradation. Structure-function analysis, overview | Streptomyces coelicolor |
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