| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DSJ_12675 | ybbN | DSJ_12675 | DSJ_18735 | Nitrite reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.675 |
| fxsA | hslU | DSJ_03785 | DSJ_02695 | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.435 |
| fxsA | hslV | DSJ_03785 | DSJ_02700 | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.680 |
| fxsA | ybbN | DSJ_03785 | DSJ_18735 | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.679 |
| gor | trxB | DSJ_01570 | DSJ_09465 | Glutathione-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.469 |
| gor | ybbN | DSJ_01570 | DSJ_18735 | Glutathione-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.939 |
| grpE | hslU | DSJ_07065 | DSJ_02695 | Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...] | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.885 |
| grpE | hslV | DSJ_07065 | DSJ_02700 | Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...] | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.853 |
| grpE | htpG | DSJ_07065 | DSJ_18985 | Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...] | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.819 |
| grpE | ybbN | DSJ_07065 | DSJ_18735 | Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...] | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.797 |
| hslU | fxsA | DSJ_02695 | DSJ_03785 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.435 |
| hslU | grpE | DSJ_02695 | DSJ_07065 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...] | 0.885 |
| hslU | hslV | DSJ_02695 | DSJ_02700 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| hslU | htpG | DSJ_02695 | DSJ_18985 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.842 |
| hslU | ybbN | DSJ_02695 | DSJ_18735 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.805 |
| hslV | fxsA | DSJ_02700 | DSJ_03785 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.680 |
| hslV | grpE | DSJ_02700 | DSJ_07065 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Nucleotide exchange factor GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds [...] | 0.853 |
| hslV | hslU | DSJ_02700 | DSJ_02695 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.999 |
| hslV | htpG | DSJ_02700 | DSJ_18985 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.831 |
| hslV | ybbN | DSJ_02700 | DSJ_18735 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.788 |