node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KMK65404.1 | KMK68808.1 | IMCC21224_11235 | IMCC21224_113694 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | 0.825 |
KMK65404.1 | grpE | IMCC21224_11235 | IMCC21224_11251 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | Molecular chaperone GrpE (heat shock 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. [...] | 0.496 |
KMK65404.1 | hslU | IMCC21224_11235 | IMCC21224_11298 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.631 |
KMK65404.1 | hslV | IMCC21224_11235 | IMCC21224_11299 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.825 |
KMK67571.1 | KMK68808.1 | IMCC21224_112442 | IMCC21224_113694 | Hypothetical protein. | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | 0.642 |
KMK67571.1 | dnaJ | IMCC21224_112442 | IMCC21224_11368 | 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 [...] | 0.853 |
KMK67571.1 | dnaK | IMCC21224_112442 | IMCC21224_11367 | Hypothetical protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.718 |
KMK67571.1 | groL | IMCC21224_112442 | IMCC21224_113506 | Hypothetical protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.853 |
KMK67571.1 | groS | IMCC21224_112442 | IMCC21224_113507 | Hypothetical protein. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.498 |
KMK67571.1 | grpE | IMCC21224_112442 | IMCC21224_11251 | Hypothetical protein. | Molecular chaperone GrpE (heat shock 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. [...] | 0.853 |
KMK67571.1 | hslU | IMCC21224_112442 | IMCC21224_11298 | Hypothetical protein. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.855 |
KMK67571.1 | hslV | IMCC21224_112442 | IMCC21224_11299 | Hypothetical protein. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.845 |
KMK68808.1 | KMK65404.1 | IMCC21224_113694 | IMCC21224_11235 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | 0.825 |
KMK68808.1 | KMK67571.1 | IMCC21224_113694 | IMCC21224_112442 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | Hypothetical protein. | 0.642 |
KMK68808.1 | dnaJ | IMCC21224_113694 | IMCC21224_11368 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | 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 [...] | 0.810 |
KMK68808.1 | dnaK | IMCC21224_113694 | IMCC21224_11367 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.747 |
KMK68808.1 | groL | IMCC21224_113694 | IMCC21224_113506 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.884 |
KMK68808.1 | groS | IMCC21224_113694 | IMCC21224_113507 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.719 |
KMK68808.1 | grpE | IMCC21224_113694 | IMCC21224_11251 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | Molecular chaperone GrpE (heat shock 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. [...] | 0.871 |
KMK68808.1 | hslU | IMCC21224_113694 | IMCC21224_11298 | PFAM: Thioredoxin; Tetratricopeptide repeat; TIGRFAM: thioredoxin. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.889 |