| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCH85518.1 | CCH87155.1 | MODMU_0046 | MODMU_1716 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Clp domain protein; Function of strongly homologous gene; enzyme. | 0.889 |
| CCH85518.1 | dnaJ | MODMU_0046 | MODMU_1760 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 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. 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 interaction [...] | 0.987 |
| CCH85518.1 | dnaJ-2 | MODMU_0046 | MODMU_5177 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Chaperone protein dnaJ, heat shock protein (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. 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 [...] | 0.986 |
| CCH85518.1 | grpE | MODMU_0046 | MODMU_5178 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Molecular chaperone GrpE (Heat shock protein); 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. [...] | 0.990 |
| CCH85518.1 | hrcA | MODMU_0046 | MODMU_1759 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Heat-inducible transcription repressor hrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.889 |
| CCH85518.1 | hspR | MODMU_0046 | MODMU_5176 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Heat shock regulator; Function of strongly homologous gene; regulator. | 0.667 |
| CCH87155.1 | CCH85518.1 | MODMU_1716 | MODMU_0046 | Clp domain protein; Function of strongly homologous gene; enzyme. | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.889 |
| CCH87155.1 | dnaJ | MODMU_1716 | MODMU_1760 | Clp domain protein; Function of strongly homologous gene; enzyme. | 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. 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 interaction [...] | 0.599 |
| CCH87155.1 | dnaJ-2 | MODMU_1716 | MODMU_5177 | Clp domain protein; Function of strongly homologous gene; enzyme. | Chaperone protein dnaJ, heat shock protein (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. 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 [...] | 0.599 |
| CCH87155.1 | dnaK | MODMU_1716 | MODMU_5179 | Clp domain protein; Function of strongly homologous gene; enzyme. | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.889 |
| CCH87155.1 | grpE | MODMU_1716 | MODMU_5178 | Clp domain protein; Function of strongly homologous gene; enzyme. | Molecular chaperone GrpE (Heat shock protein); 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. [...] | 0.821 |
| CCH87155.1 | hrcA | MODMU_1716 | MODMU_1759 | Clp domain protein; Function of strongly homologous gene; enzyme. | Heat-inducible transcription repressor hrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.585 |
| CCH87155.1 | hspR | MODMU_1716 | MODMU_5176 | Clp domain protein; Function of strongly homologous gene; enzyme. | Heat shock regulator; Function of strongly homologous gene; regulator. | 0.613 |
| CCH87155.1 | secG | MODMU_1716 | MODMU_3625 | Clp domain protein; Function of strongly homologous gene; enzyme. | Protein-export membrane protein secG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | 0.509 |
| CCH90553.1 | dnaJ-2 | MODMU_5175 | MODMU_5177 | Transcriptional regulator, MarR family (modular protein); Function of strongly homologous gene; regulator. | Chaperone protein dnaJ, heat shock protein (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. 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 [...] | 0.775 |
| CCH90553.1 | dnaK | MODMU_5175 | MODMU_5179 | Transcriptional regulator, MarR family (modular protein); Function of strongly homologous gene; regulator. | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.460 |
| CCH90553.1 | grpE | MODMU_5175 | MODMU_5178 | Transcriptional regulator, MarR family (modular protein); Function of strongly homologous gene; regulator. | Molecular chaperone GrpE (Heat shock protein); 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. [...] | 0.561 |
| CCH90553.1 | hspR | MODMU_5175 | MODMU_5176 | Transcriptional regulator, MarR family (modular protein); Function of strongly homologous gene; regulator. | Heat shock regulator; Function of strongly homologous gene; regulator. | 0.773 |
| CCH90558.1 | dnaK | MODMU_5180 | MODMU_5179 | Putative Fe-S oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.494 |
| CCH90558.1 | grpE | MODMU_5180 | MODMU_5178 | Putative Fe-S oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Molecular chaperone GrpE (Heat shock protein); 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. [...] | 0.532 |
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