| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ06061.1 | EAQ07753.1 | SKA53_08146 | SKA53_12988 | Hypothetical protein; COG0642 Signal transduction histidine kinase. | COG3118 Thioredoxin domain-containing protein. | 0.427 |
| EAQ06061.1 | ftsH | SKA53_08146 | SKA53_08551 | Hypothetical protein; COG0642 Signal transduction histidine kinase. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.480 |
| EAQ06061.1 | htpX | SKA53_08146 | SKA53_08161 | Hypothetical protein; COG0642 Signal transduction histidine kinase. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.620 |
| EAQ06061.1 | secY | SKA53_08146 | SKA53_13441 | Hypothetical protein; COG0642 Signal transduction histidine kinase. | Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.414 |
| EAQ07035.1 | htpX | SKA53_01526 | SKA53_08161 | COG0670 Integral membrane protein, interacts with FtsH; Belongs to the BI1 family. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.540 |
| EAQ07539.1 | EAQ07753.1 | SKA53_11918 | SKA53_12988 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | COG3118 Thioredoxin domain-containing protein. | 0.804 |
| EAQ07539.1 | grpE | SKA53_11918 | SKA53_11833 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | Co-chaperone 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-depend [...] | 0.414 |
| EAQ07539.1 | hslU | SKA53_11918 | SKA53_11943 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | ATP-dependent protease ATP-binding 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. | 0.543 |
| EAQ07539.1 | htpX | SKA53_11918 | SKA53_08161 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.560 |
| EAQ07753.1 | EAQ06061.1 | SKA53_12988 | SKA53_08146 | COG3118 Thioredoxin domain-containing protein. | Hypothetical protein; COG0642 Signal transduction histidine kinase. | 0.427 |
| EAQ07753.1 | EAQ07539.1 | SKA53_12988 | SKA53_11918 | COG3118 Thioredoxin domain-containing protein. | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | 0.804 |
| EAQ07753.1 | dnaJ | SKA53_12988 | SKA53_11638 | COG3118 Thioredoxin domain-containing protein. | Chaperone, 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, DnaK and [...] | 0.720 |
| EAQ07753.1 | groS | SKA53_12988 | SKA53_08661 | COG3118 Thioredoxin domain-containing protein. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.569 |
| EAQ07753.1 | grpE | SKA53_12988 | SKA53_11833 | COG3118 Thioredoxin domain-containing protein. | Co-chaperone 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-depend [...] | 0.893 |
| EAQ07753.1 | hslU | SKA53_12988 | SKA53_11943 | COG3118 Thioredoxin domain-containing protein. | ATP-dependent protease ATP-binding 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. | 0.870 |
| EAQ07753.1 | htpX | SKA53_12988 | SKA53_08161 | COG3118 Thioredoxin domain-containing protein. | Heat shock protein HtpX; COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.563 |
| dnaJ | EAQ07753.1 | SKA53_11638 | SKA53_12988 | Chaperone, 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, DnaK and [...] | COG3118 Thioredoxin domain-containing protein. | 0.720 |
| dnaJ | ftsH | SKA53_11638 | SKA53_08551 | Chaperone, 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, DnaK and [...] | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.786 |
| dnaJ | groS | SKA53_11638 | SKA53_08661 | Chaperone, 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, DnaK and [...] | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.894 |
| dnaJ | grpE | SKA53_11638 | SKA53_11833 | Chaperone, 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, DnaK and [...] | Co-chaperone 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-depend [...] | 0.988 |
