node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABP70453.1 | dnaJ | Rsph17025_1559 | Rsph17025_2765 | PFAM: RNA-binding S4 domain protein. | Chaperone protein 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, D [...] | 0.598 |
ABP70453.1 | grpE | Rsph17025_1559 | Rsph17025_2656 | PFAM: RNA-binding S4 domain protein. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.647 |
ABP70453.1 | hslU | Rsph17025_1559 | Rsph17025_2948 | PFAM: RNA-binding S4 domain protein. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.680 |
ABP70453.1 | hslV | Rsph17025_1559 | Rsph17025_2949 | PFAM: RNA-binding S4 domain protein. | 20S proteasome, A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.883 |
ABP70453.1 | lon | Rsph17025_1559 | Rsph17025_1158 | PFAM: RNA-binding S4 domain protein. | ATP-dependent protease La; 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. | 0.440 |
ABP71562.1 | ABP71780.1 | Rsph17025_2675 | Rsph17025_2894 | PFAM: FxsA cytoplasmic membrane protein. | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | 0.862 |
ABP71562.1 | grpE | Rsph17025_2675 | Rsph17025_2656 | PFAM: FxsA cytoplasmic membrane protein. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.438 |
ABP71562.1 | hslU | Rsph17025_2675 | Rsph17025_2948 | PFAM: FxsA cytoplasmic membrane protein. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.536 |
ABP71562.1 | hslV | Rsph17025_2675 | Rsph17025_2949 | PFAM: FxsA cytoplasmic membrane protein. | 20S proteasome, A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.862 |
ABP71780.1 | ABP71562.1 | Rsph17025_2894 | Rsph17025_2675 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | PFAM: FxsA cytoplasmic membrane protein. | 0.862 |
ABP71780.1 | dnaJ | Rsph17025_2894 | Rsph17025_2765 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | Chaperone protein 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, D [...] | 0.830 |
ABP71780.1 | dnaK | Rsph17025_2894 | Rsph17025_2766 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.692 |
ABP71780.1 | groL | Rsph17025_2894 | Rsph17025_2189 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.796 |
ABP71780.1 | groS | Rsph17025_2894 | Rsph17025_2190 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.659 |
ABP71780.1 | grpE | Rsph17025_2894 | Rsph17025_2656 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.909 |
ABP71780.1 | hslU | Rsph17025_2894 | Rsph17025_2948 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.912 |
ABP71780.1 | hslV | Rsph17025_2894 | Rsph17025_2949 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | 20S proteasome, A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.906 |
ABP71780.1 | lon | Rsph17025_2894 | Rsph17025_1158 | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | ATP-dependent protease La; 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. | 0.670 |
dnaJ | ABP70453.1 | Rsph17025_2765 | Rsph17025_1559 | Chaperone protein 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, D [...] | PFAM: RNA-binding S4 domain protein. | 0.598 |
dnaJ | ABP71780.1 | Rsph17025_2765 | Rsph17025_2894 | Chaperone protein 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, D [...] | TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4; Thioredoxin domain. | 0.830 |