| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANV97428.1 | ANV97466.1 | BBW65_00730 | BBW65_00940 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.785 |
| ANV97428.1 | ANV97773.1 | BBW65_00730 | BBW65_02680 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | DnaJ family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.838 |
| ANV97428.1 | dnaJ | BBW65_00730 | BBW65_03530 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 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, [...] | 0.874 |
| ANV97428.1 | dnaK | BBW65_00730 | BBW65_06830 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
| ANV97428.1 | groL | BBW65_00730 | BBW65_05025 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.750 |
| ANV97428.1 | groS | BBW65_00730 | BBW65_05020 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.778 |
| ANV97428.1 | hslV | BBW65_00730 | BBW65_00945 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.710 |
| ANV97428.1 | htpG | BBW65_00730 | BBW65_03415 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.916 |
| ANV97466.1 | ANV97428.1 | BBW65_00940 | BBW65_00730 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.785 |
| ANV97466.1 | ANV97773.1 | BBW65_00940 | BBW65_02680 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | DnaJ family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.673 |
| ANV97466.1 | dnaJ | BBW65_00940 | BBW65_03530 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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, [...] | 0.932 |
| ANV97466.1 | dnaK | BBW65_00940 | BBW65_06830 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.821 |
| ANV97466.1 | groL | BBW65_00940 | BBW65_05025 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.921 |
| ANV97466.1 | groS | BBW65_00940 | BBW65_05020 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.905 |
| ANV97466.1 | hslV | BBW65_00940 | BBW65_00945 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| ANV97466.1 | htpG | BBW65_00940 | BBW65_03415 | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.902 |
| ANV97548.1 | ANV97773.1 | BBW65_01420 | BBW65_02680 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | DnaJ family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.715 |
| ANV97548.1 | ANV98496.1 | BBW65_01420 | BBW65_06680 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.817 |
| ANV97548.1 | dnaJ | BBW65_01420 | BBW65_03530 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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, [...] | 0.673 |
| ANV97548.1 | dnaK | BBW65_01420 | BBW65_06830 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.864 |