| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LBAT_0056 | trxA | LBAT_0056 | LBAT_0472 | Ribonucleoside triphosphate reductase. | Thioredoxin; Belongs to the thioredoxin family. | 0.685 |
| LBAT_0489 | trxA | LBAT_0489 | LBAT_0472 | Thioredoxin reductase. | Thioredoxin; Belongs to the thioredoxin family. | 0.866 |
| LBAT_0489 | trxB | LBAT_0489 | LBAT_1152 | Thioredoxin reductase. | Thioredoxin reductase. | 0.443 |
| LBAT_1283 | trxA | LBAT_1283 | LBAT_0472 | Thiol peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Thioredoxin; Belongs to the thioredoxin family. | 0.675 |
| LBAT_1283 | trxB | LBAT_1283 | LBAT_1152 | Thiol peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Thioredoxin reductase. | 0.653 |
| fusA | gap | LBAT_0353 | LBAT_1137 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.789 |
| fusA | groL | LBAT_0353 | LBAT_0456 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.822 |
| fusA | trxA | LBAT_0353 | LBAT_0472 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | Thioredoxin; Belongs to the thioredoxin family. | 0.612 |
| gap | fusA | LBAT_1137 | LBAT_0353 | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | 0.789 |
| gap | groL | LBAT_1137 | LBAT_0456 | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.743 |
| gap | groS | LBAT_1137 | LBAT_0455 | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.540 |
| gap | trxA | LBAT_1137 | LBAT_0472 | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Thioredoxin; Belongs to the thioredoxin family. | 0.536 |
| groL | fusA | LBAT_0456 | LBAT_0353 | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | 0.822 |
| groL | gap | LBAT_0456 | LBAT_1137 | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.743 |
| groL | groS | LBAT_0456 | LBAT_0455 | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
| groL | grpE | LBAT_0456 | LBAT_0712 | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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- [...] | 0.988 |
| groL | trxA | LBAT_0456 | LBAT_0472 | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin; Belongs to the thioredoxin family. | 0.795 |
| groS | gap | LBAT_0455 | LBAT_1137 | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.540 |
| groS | groL | LBAT_0455 | LBAT_0456 | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| groS | grpE | LBAT_0455 | LBAT_0712 | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 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- [...] | 0.969 |