| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALO41520.1 | dnaJ | PP2015_1002 | PP2015_4142 | Chaperone; Pfam:pfam00012 Hsp70 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 [...] | 0.835 |
| ALO41520.1 | groL | PP2015_1002 | PP2015_239 | Chaperone; Pfam:pfam00012 Hsp70 protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.903 |
| ALO41520.1 | groS | PP2015_1002 | PP2015_238 | Chaperone; Pfam:pfam00012 Hsp70 protein. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.878 |
| ALO41520.1 | grpE | PP2015_1002 | PP2015_1883 | Chaperone; Pfam:pfam00012 Hsp70 protein. | 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-dependent i [...] | 0.946 |
| ALO41520.1 | hslU | PP2015_1002 | PP2015_3013 | Chaperone; Pfam:pfam00012 Hsp70 protein. | ATP-dependent protease 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. | 0.511 |
| ALO41520.1 | htpG | PP2015_1002 | PP2015_1932 | Chaperone; Pfam:pfam00012 Hsp70 protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.902 |
| ALO41520.1 | lon | PP2015_1002 | PP2015_2541 | Chaperone; Pfam:pfam00012 Hsp70 protein. | 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. | 0.596 |
| ALO43012.1 | dnaJ | PP2015_2522 | PP2015_4142 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | 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 [...] | 0.733 |
| ALO43012.1 | dnaK | PP2015_2522 | PP2015_4141 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.459 |
| ALO43012.1 | groL | PP2015_2522 | PP2015_239 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.899 |
| ALO43012.1 | groS | PP2015_2522 | PP2015_238 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.549 |
| ALO43012.1 | grpE | PP2015_2522 | PP2015_1883 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | 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-dependent i [...] | 0.912 |
| ALO43012.1 | hscA | PP2015_2522 | PP2015_2903 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | HscA-like protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.459 |
| ALO43012.1 | hslU | PP2015_2522 | PP2015_3013 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | ATP-dependent protease 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 |
| ALO43012.1 | htpG | PP2015_2522 | PP2015_1932 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.780 |
| ALO43012.1 | lon | PP2015_2522 | PP2015_2541 | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | 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. | 0.555 |
| dnaJ | ALO41520.1 | PP2015_4142 | PP2015_1002 | 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; Pfam:pfam00012 Hsp70 protein. | 0.835 |
| dnaJ | ALO43012.1 | PP2015_4142 | PP2015_2522 | 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 [...] | Thioredoxin-like protein; Pfam:pfam14561 Tetratricopeptide repeat. | 0.733 |
| dnaJ | dnaK | PP2015_4142 | PP2015_4141 | 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 |
| dnaJ | groL | PP2015_4142 | PP2015_239 | 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 [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.982 |
