| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rv1488 | Rv2867c | Rv1488 | Rv2867c | Rv1488, (MTCY277.09), len: 381 aa. Possible exported conserved protein; contains possible N-terminal signal sequence. Similar to YBBK_ECOLI|P77367 hypothetical protein ybbK from Escherichia coli (305 aa), FASTA scores: opt: 716, E(): 0, (37.1% identity in 307 aa overlap). Similar to stomatin-like proteins e.g. AF065260|AF065260_1 Clostridium difficile (320 aa), FASTA scores: opt: 767, E(): 0, (42.3% identity in 307 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | GCN5-related N-acetyltransferase; Rv2867c, (MTV003.13c), len: 284 aa. Probable acetyltransferase. Contains GNAT (Gcn5-related N-acetyltransferase) domain in C-terminal part. See Vetting et al. 2005. Similar to others e.g. Q9KYR8|SC5H4.21 hypothetical 31.3 KDA protein from Streptomyces coelicolor (287 aa), FASTA scores: opt: 798, E(): 2.4e-45, (47.95% identity in 269 aa overlap). | 0.747 |
| Rv1488 | mpa | Rv1488 | Rv2115c | Rv1488, (MTCY277.09), len: 381 aa. Possible exported conserved protein; contains possible N-terminal signal sequence. Similar to YBBK_ECOLI|P77367 hypothetical protein ybbK from Escherichia coli (305 aa), FASTA scores: opt: 716, E(): 0, (37.1% identity in 307 aa overlap). Similar to stomatin-like proteins e.g. AF065260|AF065260_1 Clostridium difficile (320 aa), FASTA scores: opt: 767, E(): 0, (42.3% identity in 307 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | Mycobacterial proteasome ATPase Mpa; 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. Is required but not sufficient to confer resistance against the lethal effects of reactiv [...] | 0.817 |
| Rv2867c | Rv1488 | Rv2867c | Rv1488 | GCN5-related N-acetyltransferase; Rv2867c, (MTV003.13c), len: 284 aa. Probable acetyltransferase. Contains GNAT (Gcn5-related N-acetyltransferase) domain in C-terminal part. See Vetting et al. 2005. Similar to others e.g. Q9KYR8|SC5H4.21 hypothetical 31.3 KDA protein from Streptomyces coelicolor (287 aa), FASTA scores: opt: 798, E(): 2.4e-45, (47.95% identity in 269 aa overlap). | Rv1488, (MTCY277.09), len: 381 aa. Possible exported conserved protein; contains possible N-terminal signal sequence. Similar to YBBK_ECOLI|P77367 hypothetical protein ybbK from Escherichia coli (305 aa), FASTA scores: opt: 716, E(): 0, (37.1% identity in 307 aa overlap). Similar to stomatin-like proteins e.g. AF065260|AF065260_1 Clostridium difficile (320 aa), FASTA scores: opt: 767, E(): 0, (42.3% identity in 307 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008). | 0.747 |
| Rv2867c | mpa | Rv2867c | Rv2115c | GCN5-related N-acetyltransferase; Rv2867c, (MTV003.13c), len: 284 aa. Probable acetyltransferase. Contains GNAT (Gcn5-related N-acetyltransferase) domain in C-terminal part. See Vetting et al. 2005. Similar to others e.g. Q9KYR8|SC5H4.21 hypothetical 31.3 KDA protein from Streptomyces coelicolor (287 aa), FASTA scores: opt: 798, E(): 2.4e-45, (47.95% identity in 269 aa overlap). | Mycobacterial proteasome ATPase Mpa; 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. Is required but not sufficient to confer resistance against the lethal effects of reactiv [...] | 0.789 |
| bpa | dop | Rv3780 | Rv2112c | Conserved 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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. | 0.774 |
| bpa | mpa | Rv3780 | Rv2115c | Conserved 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | Mycobacterial proteasome ATPase Mpa; 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. Is required but not sufficient to confer resistance against the lethal effects of reactiv [...] | 0.982 |
| bpa | pafA | Rv3780 | Rv2097c | Conserved 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | Proteasome accessory factor a PafA; 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 involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types. | 0.822 |
| bpa | prcA | Rv3780 | Rv2109c | Conserved 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | Proteasome alpha subunit PrcA; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...] | 0.987 |
| bpa | prcB | Rv3780 | Rv2110c | Conserved 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | Proteasome beta subunit PrcB; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...] | 0.959 |
| bpa | pup | Rv3780 | Rv2111c | Conserved 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | Prokaryotic ubiquitin-like protein Pup; 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 FabD, PanB and Mpa proteins. Belongs to the prokaryotic ubiquitin-like protein family. | 0.689 |
| dop | bpa | Rv2112c | Rv3780 | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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 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. Can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome; Belongs to the Bpa family. | 0.774 |
| dop | mpa | Rv2112c | Rv2115c | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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. | Mycobacterial proteasome ATPase Mpa; 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. Is required but not sufficient to confer resistance against the lethal effects of reactiv [...] | 0.942 |
| dop | pafA | Rv2112c | Rv2097c | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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 accessory factor a PafA; 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 involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types. | 0.717 |
| dop | prcA | Rv2112c | Rv2109c | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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 PrcA; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...] | 0.972 |
| dop | prcB | Rv2112c | Rv2110c | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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 PrcB; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...] | 0.974 |
| dop | pup | Rv2112c | Rv2111c | Deamidase of pup Dop; Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus 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. | Prokaryotic ubiquitin-like protein Pup; 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 FabD, PanB and Mpa proteins. Belongs to the prokaryotic ubiquitin-like protein family. | 0.956 |
| glpK | mec | Rv3696c | Rv1334 | Probable glycerol kinase GlpK (ATP:glycerol 3-phosphotransferase) (glycerokinase) (GK); 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. | Possible hydrolase; Protease that hydrolyzes the covalent CysO-cysteine adduct synthesized by CysM to release L-cysteine and regenerate CysO. | 0.937 |
| glpK | mpa | Rv3696c | Rv2115c | Probable glycerol kinase GlpK (ATP:glycerol 3-phosphotransferase) (glycerokinase) (GK); 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. | Mycobacterial proteasome ATPase Mpa; 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. Is required but not sufficient to confer resistance against the lethal effects of reactiv [...] | 0.948 |
| glpK | prcA | Rv3696c | Rv2109c | Probable glycerol kinase GlpK (ATP:glycerol 3-phosphotransferase) (glycerokinase) (GK); 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. | Proteasome alpha subunit PrcA; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...] | 0.853 |
| glpK | prcB | Rv3696c | Rv2110c | Probable glycerol kinase GlpK (ATP:glycerol 3-phosphotransferase) (glycerokinase) (GK); 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. | Proteasome beta subunit PrcB; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability [...] | 0.853 |
