node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mmc1_1650 | Mmc1_2134 | Mmc1_1650 | Mmc1_2134 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | KEGG: dps:DP1989 hypothetical protein. | 0.817 |
Mmc1_1650 | dnaK | Mmc1_1650 | Mmc1_0510 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.960 |
Mmc1_1650 | groL | Mmc1_1650 | Mmc1_0295 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.809 |
Mmc1_1650 | groS | Mmc1_1650 | Mmc1_0296 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.761 |
Mmc1_1650 | grpE | Mmc1_1650 | Mmc1_0509 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | 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 [...] | 0.912 |
Mmc1_1650 | hscA | Mmc1_1650 | Mmc1_3058 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.957 |
Mmc1_1650 | hslU | Mmc1_1650 | Mmc1_0015 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | 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. | 0.617 |
Mmc1_1650 | hslV | Mmc1_1650 | Mmc1_0017 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.552 |
Mmc1_1650 | htpG | Mmc1_1650 | Mmc1_1694 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.901 |
Mmc1_2134 | Mmc1_1650 | Mmc1_2134 | Mmc1_1650 | KEGG: dps:DP1989 hypothetical protein. | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: noc:Noc_1382 heat shock protein DnaJ-like. | 0.817 |
Mmc1_2134 | dnaJ | Mmc1_2134 | Mmc1_0511 | KEGG: dps:DP1989 hypothetical 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 [...] | 0.817 |
Mmc1_2134 | groL | Mmc1_2134 | Mmc1_0295 | KEGG: dps:DP1989 hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.860 |
Mmc1_2134 | groS | Mmc1_2134 | Mmc1_0296 | KEGG: dps:DP1989 hypothetical protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.840 |
Mmc1_2134 | grpE | Mmc1_2134 | Mmc1_0509 | KEGG: dps:DP1989 hypothetical 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 [...] | 0.921 |
Mmc1_2134 | hslU | Mmc1_2134 | Mmc1_0015 | KEGG: dps:DP1989 hypothetical 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. | 0.566 |
Mmc1_2134 | hslV | Mmc1_2134 | Mmc1_0017 | KEGG: dps:DP1989 hypothetical protein. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.570 |
Mmc1_2134 | htpG | Mmc1_2134 | Mmc1_1694 | KEGG: dps:DP1989 hypothetical protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.970 |
dnaJ | Mmc1_2134 | Mmc1_0511 | Mmc1_2134 | 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 [...] | KEGG: dps:DP1989 hypothetical protein. | 0.817 |
dnaJ | dnaK | Mmc1_0511 | Mmc1_0510 | 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. | 0.997 |
dnaJ | groL | Mmc1_0511 | Mmc1_0295 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.923 |