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N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
additional information
?
-
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[His6-myo-inositol-1-phosphate synthetase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [His6-myo-inositol-1-phosphate synthetase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
-
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
the enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
the enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-fluorescein-5-carboxamide-L-lysine + H2O
[prokaryotic ubiquitin-like protein]-L-lysine + 5-carboxyfluorescein
-
hydrolysis of the isopeptide bond in Pup-Fl and release the fluorescein-5-carboxamide lysine moiety
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the deamidase activity (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. The enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the deamidase activity (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. The enzyme catalyzes the nucleophilic attack of water on the terminal carbonyl atom of Pup, releasing ammonium in the case of deamidation or the substrate lysine in case of depupylation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
-
-
-
?
additional information
?
-
the enzyme is unable to hydrolyze linear Pup-substrate fusions
-
-
?
additional information
?
-
-
the enzyme is unable to hydrolyze linear Pup-substrate fusions
-
-
?
additional information
?
-
enzyme acts as a depupylase in the Pup proteasome system in vivo and in vitro. Dop removes prokaryotic ubiquitin-like protein Pup from substrates by specific cleavage of the isopeptide bond
-
-
?
additional information
?
-
the enzyme is unable to hydrolyze linear Pup-substrate fusions
-
-
?
additional information
?
-
enzyme acts as a depupylase in the Pup proteasome system in vivo and in vitro. Dop removes prokaryotic ubiquitin-like protein Pup from substrates by specific cleavage of the isopeptide bond
-
-
?
additional information
?
-
steric hindrance in positioning the isopeptide bond in the active site of Dop might be responsible for the observed differences in depupylation rather than differences in the overall affinity of pupylated substrate for Dop
-
-
?
additional information
?
-
steric hindrance in positioning the isopeptide bond in the active site of Dop might be responsible for the observed differences in depupylation rather than differences in the overall affinity of pupylated substrate for Dop
-
-
?
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[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
deamidase (Dop) renders prokaryotic ubiquitin-like protein Pup competent for conjugation to substrates, which is then carried out by the Pup-ligase PafA. Pupylation is a signal for proteasomal degradation in bacteria
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates the carboxyl-terminal glutamine of Pup to glutamate, preparing it for ligation to target proteins by proteasome accessory factor A (PafA)
-
-
?
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O
[prokaryotic ubiquitin-like protein]-L-glutamate + NH3
the enzyme deamidates prokaryotic ubiquitin-like protein (Pup) on the C-terminal glutamine, thereby rendering Pup competent for conjugation
-
-
?
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malfunction
generation of a dop deletion mutant in Mycobacterium smegmatis. In the Ddop strain, pupylation is severely impaired and the steady-state levels of proteasomal substrate proteins is drastically increased
malfunction
-
generation of a dop deletion mutant in Mycobacterium smegmatis. In the Ddop strain, pupylation is severely impaired and the steady-state levels of proteasomal substrate proteins is drastically increased
-
metabolism
pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination
metabolism
the enzyme is critical for the full virulence of Mycobacterium tuberculosis
metabolism
the enzyme is involved in pupylation
metabolism
the enzyme is involved in targeted proteasomal degradation
metabolism
-
PafA and depupylase Dop are each required for the full virulence of Mycobacterium tuberculosis
metabolism
-
the enzyme is essential for the infectivity of Mycobacterium tuberculosisis
metabolism
tight Pup binding and the limited degree of interaction of the enzyme (Dop) with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by this enzyme. Under starvation conditions, when accelerated protein pupylation is required, this bias is intensified by depletion of free Dop molecules, thereby minimizing the chance of depupylation. In contrast to Dop (deamidase of Pup), PafA (proteasome accessory factor A), presents a distinct preference for highmolecular-weight protein substrates. As such, PafA and Dop act in concert, rather than canceling each other's activity, to generate a high-molecular-weight pupylome. This bias in pupylome molecular weight distribution is consistent with the proposed nutritional role of the Pup-proteasome system (PPS) under starvation conditions
metabolism
-
the enzyme is involved in targeted proteasomal degradation
-
metabolism
-
tight Pup binding and the limited degree of interaction of the enzyme (Dop) with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by this enzyme. Under starvation conditions, when accelerated protein pupylation is required, this bias is intensified by depletion of free Dop molecules, thereby minimizing the chance of depupylation. In contrast to Dop (deamidase of Pup), PafA (proteasome accessory factor A), presents a distinct preference for highmolecular-weight protein substrates. As such, PafA and Dop act in concert, rather than canceling each other's activity, to generate a high-molecular-weight pupylome. This bias in pupylome molecular weight distribution is consistent with the proposed nutritional role of the Pup-proteasome system (PPS) under starvation conditions
-
metabolism
-
the enzyme is critical for the full virulence of Mycobacterium tuberculosis
-
metabolism
-
the enzyme is involved in pupylation
-
metabolism
-
pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination
-
physiological function
the enzyme is involved in pupylation. Pupylation is a signal for proteasomal degradation in bacteria
physiological function
the enzyme is required for full virulence of Mycobacterium tuberculosis
physiological function
the depupylation reaction can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa
physiological function
-
increased levels of Dop rescues pupylated substrates from destruction by removal of Pup
physiological function
-
the Pup-proteasome enzymes are essential for full virulence and persistence in the mammalian host
physiological function
-
the depupylation reaction can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa
-
physiological function
-
the enzyme is involved in pupylation. Pupylation is a signal for proteasomal degradation in bacteria
-
physiological function
-
the enzyme is required for full virulence of Mycobacterium tuberculosis
-
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Striebel, F.; Imkamp, F.; zcelik, D.; Weber-Ban, E.
Pupylation as a signal for proteasomal degradation in bacteria
Biochim. Biophys. Acta
1843
103-113
2014
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Burns, K.E.; McAllister, F.E.; Schwerdtfeger, C.; Mintseris, J.; Cerda-Maira, F.; Noens, E.E.; Wilmanns, M.; Hubbard, S.R.; Melandri, F.; Ovaa, H.; Gygi, S.P.; Darwin, K.H.
Mycobacterium tuberculosis prokaryotic ubiquitin-like protein-deconjugating enzyme is an unusual aspartate amidase
J. Biol. Chem.
287
37522-37529
2012
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Burns, K.E.; Cerda-Maira, F.A.; Wang, T.; Li, H.; Bishai, W.R.; Darwin, K.H.
"Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates
Mol. Cell.
39
821-827
2010
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Imkamp, F.; Rosenberger, T.; Striebel, F.; Keller, P.M.; Amstutz, B.; Sander, P.; Weber-Ban, E.
Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo
Mol. Microbiol.
75
744-754
2010
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
Cerda-Maira, F.A.; Pearce, M.J.; Fuortes, M.; Bishai, W.R.; Hubbard, S.R.; Darwin, K.H.
Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis
Mol. Microbiol.
77
1123-1135
2010
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
zcelik, D.; Barandun, J.; Schmitz, N.; Sutter, M.; Guth, E.; Damberger, F.F.; Allain, F.H.; Ban, N.; Weber-Ban, E.
Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway
Nat. Commun.
3
1014
2012
Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus (A0LU49), Acidothermus cellulolyticus ATCC 43068 (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU49)
brenda
Striebel, F.; Imkamp, F.; Sutter, M.; Steiner, M.; Mamedov, A.; Weber-Ban, E.
Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
Nat. Struct. Mol. Biol.
16
647-651
2009
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WNU9)
brenda
Hecht, N.; Gur, E.
Development of a fluorescence anisotropy-based assay for Dop, the first enzyme in the pupylation pathway
Anal. Biochem.
485
97-101
2015
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
Imkamp, F.; Striebel, F.; Sutter, M.; Ozcelik, D.; Zimmermann, N.; Sander, P.; Weber-Ban, E.
Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway
EMBO Rep.
11
791-797
2010
Mycobacterium tuberculosis (P9WNU9), Mycobacterium tuberculosis H37Rv (P9WNU9)
brenda
Zhang, S.; Burns-Huang, K.; Janssen, G.; Li, H.; Ovaa, H.; Hedstrom, L.; Darwin, K.
Mycobacterium tuberculosis proteasome accessory factor A (PafA) can transfer prokaryotic ubiquitin-like protein (Pup) between substrates
mBio
8
e00122-17
2017
Mycolicibacterium smegmatis
brenda
Elharar, Y.; Roth, Z.; Hecht, N.; Rotkopf, R.; Khalaila, I.; Gur, E.
Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system
Proc. Natl. Acad. Sci. USA
113
E1605-E1614
2016
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda
Hecht, N.; Gur, E.
Development of a fluorescence anisotropy-based assay for Dop, the first enzyme in the pupylation pathway
Anal. Biochem.
485
97-101
2015
Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus 11B (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU48)
brenda
Eustis, I.C.; Huang, J.; Pilkerton, M.E.; Whedon, S.D.; Chatterjee, C.
A time-resolved Foerster resonance energy transfer assay to measure activity of the deamidase of the prokaryotic ubiquitin-like protein
Anal. Biochem.
487
27-29
2015
Mycobacterium tuberculosis, Corynebacterium glutamicum (Q8NQE1), Corynebacterium glutamicum ATCC 13032 (Q8NQE1)
brenda
Barandun, J.; Damberger, F.; Delley, C.; Laederach, J.; Allain, F.; Weber-Ban, E.
Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
BMC Struct. Biol.
17
1-12
2017
Mycobacterium tuberculosis
brenda
Bolten, M.; Vahlensieck, C.; Lipp, C.; Leibundgut, M.; Ban, N.; Weber-Ban, E.
Depupylase Dop requires inorganic phosphate in the active site for catalysis
J. Biol. Chem.
292
4044-4053
2017
Acidothermus cellulolyticus (A0LU48), Acidothermus cellulolyticus 11B (A0LU48), Acidothermus cellulolyticus ATCC 43068 (A0LU48)
brenda
Laederach, J.; Cui, H.; Weber-Ban, E.
Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation
PLoS ONE
14
e0215439
2019
Mycolicibacterium smegmatis (A0QZ49), Mycolicibacterium smegmatis ATCC 700084 (A0QZ49)
brenda