| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANQ20186.1 | ANQ20900.1 | BA893_00270 | BA893_04180 | 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. | 0.949 |
| ANQ20186.1 | ANQ21357.1 | BA893_00270 | BA893_06635 | 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. | 0.452 |
| ANQ20900.1 | ANQ20186.1 | BA893_04180 | BA893_00270 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutathione-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.949 |
| ANQ20900.1 | ANQ21357.1 | BA893_04180 | BA893_06635 | Co-chaperone YbbN; 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. | 0.813 |
| ANQ20900.1 | ANQ22018.1 | BA893_04180 | BA893_10210 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
| ANQ20900.1 | ANQ22866.1 | BA893_04180 | BA893_14900 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Membrane protein FxsA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.696 |
| ANQ20900.1 | dnaJ | BA893_04180 | BA893_03425 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 of ATP-dependent interactions between DnaJ, [...] | 0.664 |
| ANQ20900.1 | grpE | BA893_04180 | BA893_03410 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.830 |
| ANQ20900.1 | hslU | BA893_04180 | BA893_01510 | Co-chaperone YbbN; 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. | 0.856 |
| ANQ20900.1 | hslV | BA893_04180 | BA893_01515 | Co-chaperone YbbN; 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. | 0.847 |
| ANQ20900.1 | htpG | BA893_04180 | BA893_04245 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.714 |
| ANQ20900.1 | lon | BA893_04180 | BA893_04700 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.527 |
| ANQ21357.1 | ANQ20186.1 | BA893_06635 | BA893_00270 | Thioredoxin-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutathione-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.452 |
| ANQ21357.1 | ANQ20900.1 | BA893_06635 | BA893_04180 | Thioredoxin-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. | 0.813 |
| ANQ21357.1 | dnaJ | BA893_06635 | BA893_03425 | Thioredoxin-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 of ATP-dependent interactions between DnaJ, [...] | 0.484 |
| ANQ22018.1 | ANQ20900.1 | BA893_10210 | BA893_04180 | Cytochrome C biogenesis 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. | 0.547 |
| ANQ22866.1 | ANQ20900.1 | BA893_14900 | BA893_04180 | Membrane protein FxsA; 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. | 0.696 |
| ANQ22866.1 | hslU | BA893_14900 | BA893_01510 | Membrane protein FxsA; 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. | 0.476 |
| ANQ22866.1 | hslV | BA893_14900 | BA893_01515 | Membrane protein FxsA; 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. | 0.696 |
| dnaJ | ANQ20900.1 | BA893_03425 | BA893_04180 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 of ATP-dependent interactions between DnaJ, [...] | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.664 |