| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lrub_0981 | Lrub_0983 | Lrub_0981 | Lrub_0983 | Rhodanese domain-containing protein. | Alkaline phosphatase. | 0.664 |
| Lrub_0981 | gpsA | Lrub_0981 | Lrub_0978 | Rhodanese domain-containing protein. | Glycerol-3-phosphate dehydrogenase (NAD+); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. | 0.871 |
| Lrub_0981 | grxC | Lrub_0981 | Lrub_0980 | Rhodanese domain-containing protein. | Glutaredoxin; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | 0.946 |
| Lrub_0981 | htpX | Lrub_0981 | Lrub_0982 | Rhodanese domain-containing protein. | M48 family peptidase; Belongs to the peptidase M48B family. | 0.767 |
| Lrub_0981 | secB | Lrub_0981 | Lrub_0979 | Rhodanese domain-containing protein. | Protein-export protein SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. | 0.881 |
| Lrub_0983 | Lrub_0981 | Lrub_0983 | Lrub_0981 | Alkaline phosphatase. | Rhodanese domain-containing protein. | 0.664 |
| Lrub_0983 | gpsA | Lrub_0983 | Lrub_0978 | Alkaline phosphatase. | Glycerol-3-phosphate dehydrogenase (NAD+); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. | 0.651 |
| Lrub_0983 | grxC | Lrub_0983 | Lrub_0980 | Alkaline phosphatase. | Glutaredoxin; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | 0.658 |
| Lrub_0983 | htpX | Lrub_0983 | Lrub_0982 | Alkaline phosphatase. | M48 family peptidase; Belongs to the peptidase M48B family. | 0.783 |
| Lrub_0983 | secB | Lrub_0983 | Lrub_0979 | Alkaline phosphatase. | Protein-export protein SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. | 0.656 |
| Lrub_1202 | htpX | Lrub_1202 | Lrub_0982 | Carrier/transport protein; Belongs to the BI1 family. | M48 family peptidase; Belongs to the peptidase M48B family. | 0.597 |
| dnaJ | ftsH | Lrub_0927 | Lrub_1629 | Molecular 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, [...] | Cell division protease 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. | 0.734 |
| dnaJ | grpE | Lrub_0927 | Lrub_0925 | Molecular 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, [...] | Heat shock protein 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- [...] | 0.995 |
| dnaJ | htpX | Lrub_0927 | Lrub_0982 | Molecular 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, [...] | M48 family peptidase; Belongs to the peptidase M48B family. | 0.472 |
| dnaJ | secY | Lrub_0927 | Lrub_2489 | Molecular 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, [...] | Preprotein translocase subunit 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. | 0.464 |
| ftsH | dnaJ | Lrub_1629 | Lrub_0927 | Cell division protease 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. | Molecular 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, [...] | 0.734 |
| ftsH | grpE | Lrub_1629 | Lrub_0925 | Cell division protease 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. | Heat shock protein 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- [...] | 0.663 |
| ftsH | htpX | Lrub_1629 | Lrub_0982 | Cell division protease 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. | M48 family peptidase; Belongs to the peptidase M48B family. | 0.774 |
| ftsH | secY | Lrub_1629 | Lrub_2489 | Cell division protease 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. | Preprotein translocase subunit 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. | 0.647 |
| gpsA | Lrub_0981 | Lrub_0978 | Lrub_0981 | Glycerol-3-phosphate dehydrogenase (NAD+); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. | Rhodanese domain-containing protein. | 0.871 |
