| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cbpA | dnaK | ADJ80_09855 | ADJ80_09080 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| cbpA | groEL | ADJ80_09855 | ADJ80_01195 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.747 |
| cbpA | groES | ADJ80_09855 | ADJ80_01190 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.595 |
| cbpA | grpE | ADJ80_09855 | ADJ80_10285 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 of ATP [...] | 0.920 |
| cbpA | hscA | ADJ80_09855 | ADJ80_09950 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.936 |
| cbpA | hslU | ADJ80_09855 | ADJ80_03120 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.595 |
| cbpA | hslV | ADJ80_09855 | ADJ80_03115 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.492 |
| cbpA | htpG_1 | ADJ80_09855 | ADJ80_05600 | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.916 |
| dnaJ_2 | dnaK | ADJ80_09085 | ADJ80_09080 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| dnaJ_2 | groEL | ADJ80_09085 | ADJ80_01195 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.959 |
| dnaJ_2 | groES | ADJ80_09085 | ADJ80_01190 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.842 |
| dnaJ_2 | grpE | ADJ80_09085 | ADJ80_10285 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 of ATP [...] | 0.987 |
| dnaJ_2 | hscA | ADJ80_09085 | ADJ80_09950 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.977 |
| dnaJ_2 | hslU | ADJ80_09085 | ADJ80_03120 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.957 |
| dnaJ_2 | hslV | ADJ80_09085 | ADJ80_03115 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.932 |
| dnaJ_2 | htpG_1 | ADJ80_09085 | ADJ80_05600 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
| dnaJ_2 | ybbN | ADJ80_09085 | ADJ80_09275 | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.686 |
| dnaK | cbpA | ADJ80_09080 | ADJ80_09855 | Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| dnaK | dnaJ_2 | ADJ80_09080 | ADJ80_09085 | Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| dnaK | groEL | ADJ80_09080 | ADJ80_01195 | Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.923 |
