node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Maqu_0470 | Maqu_0795 | Maqu_0470 | Maqu_0795 | Peptidylprolyl isomerase, FKBP-type; PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase, FKBP-type; KEGG: hch:HCH_00278 FKBP-type peptidyl-prolyl cis-trans isomerases 1. | KEGG: ssn:SSO_3355 hypothetical protein. | 0.708 |
Maqu_0470 | dnaK | Maqu_0470 | Maqu_3362 | Peptidylprolyl isomerase, FKBP-type; PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase, FKBP-type; KEGG: hch:HCH_00278 FKBP-type peptidyl-prolyl cis-trans isomerases 1. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.686 |
Maqu_0470 | htpG | Maqu_0470 | Maqu_1054 | Peptidylprolyl isomerase, FKBP-type; PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase, FKBP-type; KEGG: hch:HCH_00278 FKBP-type peptidyl-prolyl cis-trans isomerases 1. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.932 |
Maqu_0795 | Maqu_0470 | Maqu_0795 | Maqu_0470 | KEGG: ssn:SSO_3355 hypothetical protein. | Peptidylprolyl isomerase, FKBP-type; PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase, FKBP-type; KEGG: hch:HCH_00278 FKBP-type peptidyl-prolyl cis-trans isomerases 1. | 0.708 |
Maqu_0795 | dnaK | Maqu_0795 | Maqu_3362 | KEGG: ssn:SSO_3355 hypothetical protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.568 |
Maqu_0795 | htpG | Maqu_0795 | Maqu_1054 | KEGG: ssn:SSO_3355 hypothetical protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.950 |
Maqu_1795 | dnaK | Maqu_1795 | Maqu_3362 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 hypothetical protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.934 |
Maqu_1795 | groL | Maqu_1795 | Maqu_2030 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.740 |
Maqu_1795 | groS | Maqu_1795 | Maqu_2031 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 hypothetical protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.545 |
Maqu_1795 | grpE | Maqu_1795 | Maqu_3363 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 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 [...] | 0.810 |
Maqu_1795 | hslU | Maqu_1795 | Maqu_0817 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 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. | 0.622 |
Maqu_1795 | hslV | Maqu_1795 | Maqu_0818 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 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. | 0.460 |
Maqu_1795 | htpG | Maqu_1795 | Maqu_1054 | PFAM: heat shock protein DnaJ domain protein; KEGG: pae:PA1191 hypothetical protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.837 |
dnaJ | dnaK | Maqu_3361 | Maqu_3362 | 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 | Maqu_3361 | Maqu_2030 | 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. | 0.939 |
dnaJ | groS | Maqu_3361 | Maqu_2031 | 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 Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.858 |
dnaJ | grpE | Maqu_3361 | Maqu_3363 | 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 [...] | 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 [...] | 0.988 |
dnaJ | hslU | Maqu_3361 | Maqu_0817 | 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 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. | 0.898 |
dnaJ | hslV | Maqu_3361 | Maqu_0818 | 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 [...] | 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. | 0.884 |
dnaJ | htpG | Maqu_3361 | Maqu_1054 | 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 Hsp90; Molecular chaperone. Has ATPase activity. | 0.951 |