| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SPO0092 | SPO2850 | SPO0092 | SPO2850 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 0.936 |
| SPO0092 | dnaJ | SPO0092 | SPO0044 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | 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 [...] | 0.941 |
| SPO0092 | groEL | SPO0092 | SPO0887 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.900 |
| SPO0092 | groES | SPO0092 | SPO0886 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.877 |
| SPO0092 | grpE | SPO0092 | SPO0010 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | Co-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-depend [...] | 0.962 |
| SPO0092 | hrcA | SPO0092 | SPO0009 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | 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. | 0.851 |
| SPO0092 | hslU | SPO0092 | SPO3882 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | ATP-dependent hsl protease, ATP-binding 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. | 0.576 |
| SPO0092 | hslV | SPO0092 | SPO3880 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.501 |
| SPO0092 | lon | SPO0092 | SPO2613 | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | 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. | 0.599 |
| SPO2850 | SPO0092 | SPO2850 | SPO0092 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | 0.936 |
| SPO2850 | dnaK | SPO2850 | SPO0043 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.955 |
| SPO2850 | groEL | SPO2850 | SPO0887 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.804 |
| SPO2850 | groES | SPO2850 | SPO0886 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.634 |
| SPO2850 | grpE | SPO2850 | SPO0010 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Co-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-depend [...] | 0.888 |
| SPO2850 | hrcA | SPO2850 | SPO0009 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 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. | 0.761 |
| SPO2850 | hslU | SPO2850 | SPO3882 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | ATP-dependent hsl protease, ATP-binding 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. | 0.687 |
| SPO2850 | hslV | SPO2850 | SPO3880 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.551 |
| SPO2850 | lon | SPO2850 | SPO2613 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 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. | 0.613 |
| dnaJ | SPO0092 | SPO0044 | SPO0092 | 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 [...] | Heat shock protein, Hsp70 family; Identified by similarity to SP:P36928. | 0.941 |
| dnaJ | dnaK | SPO0044 | SPO0043 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |