| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Amuc_0631 | htpG | Amuc_0631 | Amuc_2002 | FAD-binding domain protein; PFAM: oxidoreductase FAD/NAD(P)-binding domain protein; FAD-binding domain protein; KEGG: bld:BLi01302 YvgR. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.723 |
| Amuc_0949 | Amuc_1282 | Amuc_0949 | Amuc_1282 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase FKBP-type; KEGG: pmy:Pmen_1314 peptidylprolyl isomerase, FKBP-type. | 0.412 |
| Amuc_0949 | dnaJ | Amuc_0949 | Amuc_1460 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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 [...] | 0.931 |
| Amuc_0949 | dnaK | Amuc_0949 | Amuc_1406 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.440 |
| Amuc_0949 | groL | Amuc_0949 | Amuc_1408 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.658 |
| Amuc_0949 | htpG | Amuc_0949 | Amuc_2002 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.755 |
| Amuc_1026 | Amuc_1282 | Amuc_1026 | Amuc_1282 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase FKBP-type; KEGG: pmy:Pmen_1314 peptidylprolyl isomerase, FKBP-type. | 0.412 |
| Amuc_1026 | dnaJ | Amuc_1026 | Amuc_1460 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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 [...] | 0.931 |
| Amuc_1026 | dnaK | Amuc_1026 | Amuc_1406 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.440 |
| Amuc_1026 | htpG | Amuc_1026 | Amuc_2002 | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.755 |
| Amuc_1282 | Amuc_0949 | Amuc_1282 | Amuc_0949 | PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase FKBP-type; KEGG: pmy:Pmen_1314 peptidylprolyl isomerase, FKBP-type. | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.412 |
| Amuc_1282 | Amuc_1026 | Amuc_1282 | Amuc_1026 | PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase FKBP-type; KEGG: pmy:Pmen_1314 peptidylprolyl isomerase, FKBP-type. | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.412 |
| Amuc_1282 | dnaK | Amuc_1282 | Amuc_1406 | PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase FKBP-type; KEGG: pmy:Pmen_1314 peptidylprolyl isomerase, FKBP-type. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.786 |
| Amuc_1282 | htpG | Amuc_1282 | Amuc_2002 | PFAM: FKBP-type peptidyl-prolyl isomerase domain protein; peptidylprolyl isomerase FKBP-type; KEGG: pmy:Pmen_1314 peptidylprolyl isomerase, FKBP-type. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.900 |
| clpB | dnaJ | Amuc_0836 | Amuc_1460 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 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 [...] | 0.885 |
| clpB | dnaK | Amuc_0836 | Amuc_1406 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.987 |
| clpB | groL | Amuc_0836 | Amuc_1408 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.543 |
| clpB | groS | Amuc_0836 | Amuc_1407 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.741 |
| clpB | grpE | Amuc_0836 | Amuc_1459 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 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 [...] | 0.860 |
| clpB | htpG | Amuc_0836 | Amuc_2002 | ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.813 |