node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABK73517.1 | glpK | MSMEG_4907 | MSMEG_6229 | Identified by match to protein family HMM PF01398. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.912 |
ABK73517.1 | glpK-2 | MSMEG_4907 | MSMEG_6756 | Identified by match to protein family HMM PF01398. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.912 |
ABK73517.1 | glpK-3 | MSMEG_4907 | MSMEG_6759 | Identified by match to protein family HMM PF01398. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.912 |
ABK73517.1 | mpa | MSMEG_4907 | MSMEG_3902 | Identified by match to protein family HMM PF01398. | ATPase, AAA family protein; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | 0.990 |
ABK73517.1 | prcA | MSMEG_4907 | MSMEG_3894 | Identified by match to protein family HMM PF01398. | Proteasome alpha subunit; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin- like protein (Pup). Identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. The Pup- proteasome system (PPS) is essential for survival under starvation; PPS likely functions to recycle a [...] | 0.923 |
ABK73517.1 | prcB | MSMEG_4907 | MSMEG_3895 | Identified by match to protein family HMM PF01398. | Proteasome beta subunit; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin- like protein (Pup). Among the identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. The Pup-proteasome system (PPS) is essential for survival under starvation; PPS likely functions to r [...] | 0.923 |
bpa | dop | MSMEG_6365 | MSMEG_3897 | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | 0.704 |
bpa | mpa | MSMEG_6365 | MSMEG_3902 | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | ATPase, AAA family protein; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | 0.934 |
bpa | pafA | MSMEG_6365 | MSMEG_3890 | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | Proteasome component; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction likely involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. Belongs to the Pup ligase/Pup deamidase family. Pup- conjugating enzyme subfamily. | 0.874 |
bpa | prcA | MSMEG_6365 | MSMEG_3894 | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | Proteasome alpha subunit; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin- like protein (Pup). Identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. The Pup- proteasome system (PPS) is essential for survival under starvation; PPS likely functions to recycle a [...] | 0.990 |
bpa | prcB | MSMEG_6365 | MSMEG_3895 | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | Proteasome beta subunit; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin- like protein (Pup). Among the identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. The Pup-proteasome system (PPS) is essential for survival under starvation; PPS likely functions to r [...] | 0.979 |
bpa | pup | MSMEG_6365 | MSMEG_3896 | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | Conserved hypothetical protein; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the SodA and Ino1 proteins. | 0.778 |
dop | bpa | MSMEG_3897 | MSMEG_6365 | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction (By similarity); Belongs to the Bpa family. | 0.704 |
dop | mpa | MSMEG_3897 | MSMEG_3902 | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | ATPase, AAA family protein; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. | 0.918 |
dop | pafA | MSMEG_3897 | MSMEG_3890 | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | Proteasome component; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction likely involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. Belongs to the Pup ligase/Pup deamidase family. Pup- conjugating enzyme subfamily. | 0.474 |
dop | prcA | MSMEG_3897 | MSMEG_3894 | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | Proteasome alpha subunit; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin- like protein (Pup). Identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. The Pup- proteasome system (PPS) is essential for survival under starvation; PPS likely functions to recycle a [...] | 0.957 |
dop | prcB | MSMEG_3897 | MSMEG_3895 | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | Proteasome beta subunit; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin- like protein (Pup). Among the identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. The Pup-proteasome system (PPS) is essential for survival under starvation; PPS likely functions to r [...] | 0.952 |
dop | pup | MSMEG_3897 | MSMEG_3896 | Proteasome component; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily. | Conserved hypothetical protein; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the SodA and Ino1 proteins. | 0.964 |
glpK | ABK73517.1 | MSMEG_6229 | MSMEG_4907 | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | Identified by match to protein family HMM PF01398. | 0.912 |
glpK | glpK-2 | MSMEG_6229 | MSMEG_6756 | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.905 |