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Literature summary extracted from

  • Delley, C.L.; Mueller, A.U.; Ziemski, M.; Weber-Ban, E.
    Prokaryotic ubiquitin-like protein and its ligase/deligase enzymes (2017), J. Mol. Biol., 429, 3486-3499 .
    View publication on PubMed

Application

EC Number Application Comment Organism
6.3.1.19 drug development the enzyme is a target for drug development in tuberculosis treatment Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Mycobacterium tuberculosis
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Corynebacterium glutamicum
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Bifidobacterium adolescentis
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Thermobifida fusca
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Renibacterium salmoninarum
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Salinispora tropica
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Kocuria rhizophila
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Micrococcus luteus
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Acidothermus cellulolyticus
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Mycolicibacterium smegmatis
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Rhodococcus erythropolis
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Paenarthrobacter aurescens
6.3.1.19 gene pafA, genetic arrangement in the pupylation gene locus, comparisons, overview Streptomyces coelicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.19 Mg2+ required Mycobacterium tuberculosis
6.3.1.19 Mg2+ required Corynebacterium glutamicum
6.3.1.19 Mg2+ required Bifidobacterium adolescentis
6.3.1.19 Mg2+ required Thermobifida fusca
6.3.1.19 Mg2+ required Renibacterium salmoninarum
6.3.1.19 Mg2+ required Salinispora tropica
6.3.1.19 Mg2+ required Kocuria rhizophila
6.3.1.19 Mg2+ required Micrococcus luteus
6.3.1.19 Mg2+ required Acidothermus cellulolyticus
6.3.1.19 Mg2+ required Mycolicibacterium smegmatis
6.3.1.19 Mg2+ required Rhodococcus erythropolis
6.3.1.19 Mg2+ required Paenarthrobacter aurescens
6.3.1.19 Mg2+ required Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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

EC Number Organism UniProt Comment Textmining
6.3.1.19 Acidothermus cellulolyticus A0LU53
-
-
6.3.1.19 Acidothermus cellulolyticus ATCC 43068 / 11B A0LU53
-
-
6.3.1.19 Bifidobacterium adolescentis A1A0U7
-
-
6.3.1.19 Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a A1A0U7
-
-
6.3.1.19 Corynebacterium glutamicum Q8NQE1
-
-
6.3.1.19 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 Q8NQE1
-
-
6.3.1.19 Kocuria rhizophila B2GIN9
-
-
6.3.1.19 Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201 B2GIN9
-
-
6.3.1.19 Micrococcus luteus C5CBV0 i.e. Micrococcus lysodeikticus
-
6.3.1.19 Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230 C5CBV0 i.e. Micrococcus lysodeikticus
-
6.3.1.19 Mycobacterium tuberculosis P9WNU7
-
-
6.3.1.19 Mycobacterium tuberculosis ATCC 25618 / H37Rv P9WNU7
-
-
6.3.1.19 Mycolicibacterium smegmatis A0QZ42
-
-
6.3.1.19 Mycolicibacterium smegmatis ATCC 700084 / mc2155 A0QZ42
-
-
6.3.1.19 Paenarthrobacter aurescens A1R6Q9 i.e. Arthrobacter aurescens
-
6.3.1.19 Paenarthrobacter aurescens TC1 A1R6Q9 i.e. Arthrobacter aurescens
-
6.3.1.19 Renibacterium salmoninarum A9WSH9
-
-
6.3.1.19 Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 A9WSH9
-
-
6.3.1.19 Rhodococcus erythropolis C0ZZU4
-
-
6.3.1.19 Rhodococcus erythropolis PR4 / NBRC 100887 C0ZZU4
-
-
6.3.1.19 Salinispora tropica A4X747
-
-
6.3.1.19 Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440 A4X747
-
-
6.3.1.19 Streptomyces coelicolor Q9RJ61
-
-
6.3.1.19 Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 Q9RJ61
-
-
6.3.1.19 Thermobifida fusca Q47NZ6
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a
6.3.1.19 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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
-
 ?
6.3.1.19 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

EC Number Synonyms Comment Organism
6.3.1.19 PafA
-
 Mycobacterium tuberculosis
6.3.1.19 PafA
-
 Corynebacterium glutamicum
6.3.1.19 PafA
-
 Bifidobacterium adolescentis
6.3.1.19 PafA
-
 Thermobifida fusca
6.3.1.19 PafA
-
 Renibacterium salmoninarum
6.3.1.19 PafA
-
 Salinispora tropica
6.3.1.19 PafA
-
 Kocuria rhizophila
6.3.1.19 PafA
-
 Micrococcus luteus
6.3.1.19 PafA
-
 Acidothermus cellulolyticus
6.3.1.19 PafA
-
 Mycolicibacterium smegmatis
6.3.1.19 PafA
-
 Rhodococcus erythropolis
6.3.1.19 PafA
-
 Paenarthrobacter aurescens
6.3.1.19 PafA
-
 Streptomyces coelicolor
6.3.1.19 Pup ligase
-
 Mycobacterium tuberculosis
6.3.1.19 Pup ligase
-
 Corynebacterium glutamicum
6.3.1.19 Pup ligase
-
 Bifidobacterium adolescentis
6.3.1.19 Pup ligase
-
 Thermobifida fusca
6.3.1.19 Pup ligase
-
 Renibacterium salmoninarum
6.3.1.19 Pup ligase
-
 Salinispora tropica
6.3.1.19 Pup ligase
-
 Kocuria rhizophila
6.3.1.19 Pup ligase
-
 Micrococcus luteus
6.3.1.19 Pup ligase
-
 Acidothermus cellulolyticus
6.3.1.19 Pup ligase
-
 Mycolicibacterium smegmatis
6.3.1.19 Pup ligase
-
 Rhodococcus erythropolis
6.3.1.19 Pup ligase
-
 Paenarthrobacter aurescens
6.3.1.19 Pup ligase
-
 Streptomyces coelicolor

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.19 ATP
-
 Mycobacterium tuberculosis
6.3.1.19 ATP
-
 Corynebacterium glutamicum
6.3.1.19 ATP
-
 Bifidobacterium adolescentis
6.3.1.19 ATP
-
 Thermobifida fusca
6.3.1.19 ATP
-
 Renibacterium salmoninarum
6.3.1.19 ATP
-
 Salinispora tropica
6.3.1.19 ATP
-
 Kocuria rhizophila
6.3.1.19 ATP
-
 Micrococcus luteus
6.3.1.19 ATP
-
 Acidothermus cellulolyticus
6.3.1.19 ATP
-
 Mycolicibacterium smegmatis
6.3.1.19 ATP
-
 Rhodococcus erythropolis
6.3.1.19 ATP
-
 Paenarthrobacter aurescens
6.3.1.19 ATP
-
 Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
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 Corynebacterium glutamicum
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 Bifidobacterium adolescentis
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 Thermobifida fusca
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 Renibacterium salmoninarum
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 Salinispora tropica
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 Kocuria rhizophila
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 Micrococcus luteus
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 Acidothermus cellulolyticus
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 Mycolicibacterium smegmatis
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 Rhodococcus erythropolis
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 Paenarthrobacter aurescens
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 Streptomyces coelicolor
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. Intrinsically disordered Pup is structurally unlike the stably folded ubiquitin Mycobacterium tuberculosis
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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
6.3.1.19 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