6.3.1.19: prokaryotic ubiquitin-like protein ligase
This is an abbreviated version!
For detailed information about prokaryotic ubiquitin-like protein ligase, go to the full flat file.
Word Map on EC 6.3.1.19
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6.3.1.19
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mycobacterium
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tuberculosis
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depupylation
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pup-proteasome
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actinobacteria
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depupylase
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deamidation
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ligases
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deamidase
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smegmatis
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ubiquitin-proteasome
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tcmsp
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cytoscape
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isopeptide
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genecards
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nitrospirae
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drug development
- 6.3.1.19
- mycobacterium
- tuberculosis
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depupylation
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pup-proteasome
- actinobacteria
- depupylase
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deamidation
- ligases
- deamidase
- smegmatis
-
ubiquitin-proteasome
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tcmsp
-
cytoscape
-
isopeptide
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genecards
- nitrospirae
- drug development
Reaction
Synonyms
PafA, proteasome accessory factor A, Pup ligase, Pup-protein ligase, Rv2097c, ubiquitin-like protein ligase
ECTree
6.3.1.19 prokaryotic ubiquitin-like protein ligaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 6.3.1.19 - prokaryotic ubiquitin-like protein ligase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive
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-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive
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-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Acidothermus cellulolyticus ATCC 43068 / 11B
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
key enzyme in the Pup tagging (i.e. pupylation) system. Protein pupylation can be regulated at the enzyme level via an allosteric mechanism
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-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
pupylation is a signal for proteasomal degradation in bacteria. The prokaryotic, ubiquitin-like protein (Pup) is conjugated through its C-terminal residue to lysine side chains of substrates via an isopeptide bond. Pup proteins are small, ranging from 60 to 70 residues in length with Gly-Gly-Glu or Gly-Gly-Gln as C-terminal residues. Deamidation of the C-terminal glutamine of Pup by the deamidase of Pup (Dop) renders Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
pupylation is a signal for proteasomal degradation in bacteria. The prokaryotic, ubiquitin-like protein (Pup) is conjugated through its C-terminal residue to lysine side chains of substrates via an isopeptide bond. Pup proteins are small, ranging from 60 to 70 residues in length with Gly-Gly-Glu or Gly-Gly-Gln as C-terminal residues. Deamidation of the C-terminal glutamine of Pup by the deamidase of Pup (Dop) renders Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
key enzyme in the Pup tagging (i.e. pupylation) system. Protein pupylation can be regulated at the enzyme level via an allosteric mechanism
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-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Mycolicibacterium smegmatis ATCC 700084 / mc2155
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Rhodococcus erythropolis PR4 / NBRC 100887
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-
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
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?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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-
-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]
pupylation targets the substrates for degradation by the proteasome
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-
?
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]
pupylation targets the substrates for degradation by the proteasome
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?
additional information
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PafA can pupylate itself, extra-pupylation by PafA can also occur, mostly in the form of poly-pupylation. Unlike in the eukaryotic UPS where poly-ubiquitylation is seen, in vivo targets of the Pup-proteasome system are found almost exclusively to be monopupylated, except for PafA itself. Poly-pupylation occurs via pupylation of an already pupylated target, rather than by conjugation of pre-formed poly-Pup chains
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?
additional information
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Mycolicibacterium smegmatis ATCC 700084 / mc2155
PafA can pupylate itself, extra-pupylation by PafA can also occur, mostly in the form of poly-pupylation. Unlike in the eukaryotic UPS where poly-ubiquitylation is seen, in vivo targets of the Pup-proteasome system are found almost exclusively to be monopupylated, except for PafA itself. Poly-pupylation occurs via pupylation of an already pupylated target, rather than by conjugation of pre-formed poly-Pup chains
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?
