| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KB13_1123 | KB13_382 | KB13_1123 | KB13_382 | Hypothetical protein. | Hypothetical protein. | 0.543 |
| KB13_1123 | KB13_452 | KB13_1123 | KB13_452 | Hypothetical protein. | Hypothetical protein. | 0.578 |
| KB13_1123 | htpX | KB13_1123 | KB13_548 | Hypothetical protein. | Heat shock protein HtpX; [O] COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.578 |
| KB13_382 | KB13_1123 | KB13_382 | KB13_1123 | Hypothetical protein. | Hypothetical protein. | 0.543 |
| KB13_382 | KB13_452 | KB13_382 | KB13_452 | Hypothetical protein. | Hypothetical protein. | 0.418 |
| KB13_382 | htpX | KB13_382 | KB13_548 | Hypothetical protein. | Heat shock protein HtpX; [O] COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.418 |
| KB13_452 | KB13_1123 | KB13_452 | KB13_1123 | Hypothetical protein. | Hypothetical protein. | 0.578 |
| KB13_452 | KB13_382 | KB13_452 | KB13_382 | Hypothetical protein. | Hypothetical protein. | 0.418 |
| KB13_452 | htpX | KB13_452 | KB13_548 | Hypothetical protein. | Heat shock protein HtpX; [O] COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.773 |
| KB13_526 | dnaJ | KB13_526 | KB13_927 | [R] COG0790 FOG: TPR repeat, SEL1 subfamily. | 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 [...] | 0.657 |
| KB13_526 | htpX | KB13_526 | KB13_548 | [R] COG0790 FOG: TPR repeat, SEL1 subfamily. | Heat shock protein HtpX; [O] COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.466 |
| dnaJ | KB13_526 | KB13_927 | KB13_526 | 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 [...] | [R] COG0790 FOG: TPR repeat, SEL1 subfamily. | 0.657 |
| dnaJ | groS | KB13_927 | KB13_857 | 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 GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.801 |
| dnaJ | grpE | KB13_927 | KB13_600 | 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 [...] | 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 [...] | 0.997 |
| dnaJ | hflB | KB13_927 | KB13_193 | 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 [...] | Cell division protein; 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. | 0.722 |
| dnaJ | htpX | KB13_927 | KB13_548 | 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 HtpX; [O] COG0501 Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. | 0.570 |
| dnaJ | msrC | KB13_927 | KB13_1279 | 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 [...] | Hypothetical protein; [O] COG0229 Conserved domain frequently associated with peptide methionine sulfoxide reductase; probable Secreted protein-methione-sulfoxide reductase with methionine-s-sulfoxide and methionine-r-sulfoxide reductase activity putative signal peptide msyqgliylssvailfsassva; EC_number=1.8.4.11. | 0.492 |
| dnaJ | secY | KB13_927 | KB13_481 | 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 [...] | Preprotein translocase, SecY subunit; 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. | 0.630 |
| groS | dnaJ | KB13_857 | KB13_927 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 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 [...] | 0.801 |
| groS | grpE | KB13_857 | KB13_600 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 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 [...] | 0.950 |
