| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 [...] | 0.978 |
| CCH85518.1 | groEL | MODMU_0046 | MODMU_0782 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.921 |
| CCH85518.1 | groL | MODMU_0046 | MODMU_4858 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.922 |
| 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. [...] | 0.987 |
| CCH85518.1 | gyrA | MODMU_0046 | MODMU_0011 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | DNA gyrase subunit A; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.565 |
| CCH85518.1 | gyrB | MODMU_0046 | MODMU_0010 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.521 |
| 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. | 0.611 |
| CCH85518.1 | rplM | MODMU_0046 | MODMU_4877 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 50S ribosomal subunit protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.628 |
| CCH85518.1 | rplN | MODMU_0046 | MODMU_4909 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 50S ribosomal subunit protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.729 |
| dnaJ-2 | CCH85518.1 | MODMU_5177 | MODMU_0046 | 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 [...] | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.978 |
| dnaJ-2 | dnaK | MODMU_5177 | MODMU_5179 | 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 [...] | 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. | 0.997 |
| dnaJ-2 | groEL | MODMU_5177 | MODMU_0782 | 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 [...] | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.832 |
| dnaJ-2 | groL | MODMU_5177 | MODMU_4858 | 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 [...] | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.838 |
| dnaJ-2 | grpE | MODMU_5177 | MODMU_5178 | 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 [...] | 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 |
| dnaJ-2 | gyrA | MODMU_5177 | MODMU_0011 | 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 [...] | DNA gyrase subunit A; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.816 |
| dnaJ-2 | gyrB | MODMU_5177 | MODMU_0010 | 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 [...] | DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.794 |
| dnaJ-2 | hspR | MODMU_5177 | MODMU_5176 | 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 [...] | Heat shock regulator; Function of strongly homologous gene; regulator. | 0.932 |
| dnaJ-2 | rplM | MODMU_5177 | MODMU_4877 | 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 [...] | 50S ribosomal subunit protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.797 |
| dnaJ-2 | rplN | MODMU_5177 | MODMU_4909 | 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 [...] | 50S ribosomal subunit protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.805 |
| dnaK | dnaJ-2 | MODMU_5179 | MODMU_5177 | 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. | 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 [...] | 0.997 |
