| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KGL12669.1 | KGL12675.1 | LS73_07855 | LS73_07890 | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.566 |
| KGL12669.1 | dnaJ | LS73_07855 | LS73_07600 | Molecular chaperone GroES; 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, [...] | 0.754 |
| KGL12669.1 | dnaK | LS73_07855 | LS73_07755 | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.961 |
| KGL12669.1 | groEL | LS73_07855 | LS73_02840 | Molecular chaperone GroES; 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. | 0.957 |
| KGL12669.1 | groEL-2 | LS73_07855 | LS73_07860 | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...] | 0.984 |
| KGL12669.1 | grpE | LS73_07855 | LS73_07750 | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 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- [...] | 0.896 |
| KGL12669.1 | hslU | LS73_07855 | LS73_01980 | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.805 |
| KGL12669.1 | hslV | LS73_07855 | LS73_01975 | Molecular chaperone GroES; 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. | 0.770 |
| KGL12669.1 | lon | LS73_07855 | LS73_02810 | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lon protease; 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. | 0.566 |
| KGL12675.1 | KGL12669.1 | LS73_07890 | LS73_07855 | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.566 |
| KGL12675.1 | dnaJ | LS73_07890 | LS73_07600 | Lon protease; 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, [...] | 0.808 |
| KGL12675.1 | dnaK | LS73_07890 | LS73_07755 | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.840 |
| KGL12675.1 | groEL | LS73_07890 | LS73_02840 | Lon protease; 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. | 0.774 |
| KGL12675.1 | groEL-2 | LS73_07890 | LS73_07860 | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...] | 0.774 |
| KGL12675.1 | groES | LS73_07890 | LS73_02845 | Lon protease; 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. | 0.566 |
| KGL12675.1 | grpE | LS73_07890 | LS73_07750 | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 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- [...] | 0.798 |
| KGL12675.1 | hslU | LS73_07890 | LS73_01980 | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.808 |
| KGL12675.1 | hslV | LS73_07890 | LS73_01975 | Lon protease; 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. | 0.792 |
| dnaJ | KGL12669.1 | LS73_07600 | LS73_07855 | 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, [...] | Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.754 |
| dnaJ | KGL12675.1 | LS73_07600 | LS73_07890 | 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, [...] | Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.808 |
