| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LBAT_0489 | LBAT_1627 | LBAT_0489 | LBAT_1627 | Thioredoxin reductase. | Thioredoxin; Belongs to the thioredoxin family. | 0.692 |
| LBAT_0489 | trxB | LBAT_0489 | LBAT_1152 | Thioredoxin reductase. | Thioredoxin reductase. | 0.412 |
| LBAT_0917 | LBAT_1627 | LBAT_0917 | LBAT_1627 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Thioredoxin; Belongs to the thioredoxin family. | 0.512 |
| LBAT_0917 | groL | LBAT_0917 | LBAT_0456 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.749 |
| LBAT_0917 | hslU | LBAT_0917 | LBAT_0916 | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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. | 0.999 |
| LBAT_1142 | LBAT_1627 | LBAT_1142 | LBAT_1627 | Ferric uptake regulator; Belongs to the Fur family. | Thioredoxin; Belongs to the thioredoxin family. | 0.504 |
| LBAT_1627 | LBAT_0489 | LBAT_1627 | LBAT_0489 | Thioredoxin; Belongs to the thioredoxin family. | Thioredoxin reductase. | 0.692 |
| LBAT_1627 | LBAT_0917 | LBAT_1627 | LBAT_0917 | Thioredoxin; Belongs to the thioredoxin family. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.512 |
| LBAT_1627 | LBAT_1142 | LBAT_1627 | LBAT_1142 | Thioredoxin; Belongs to the thioredoxin family. | Ferric uptake regulator; Belongs to the Fur family. | 0.504 |
| LBAT_1627 | fusA | LBAT_1627 | LBAT_0353 | Thioredoxin; Belongs to the thioredoxin 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. | 0.619 |
| LBAT_1627 | gap | LBAT_1627 | LBAT_1137 | Thioredoxin; Belongs to the thioredoxin family. | Glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.606 |
| LBAT_1627 | groL | LBAT_1627 | LBAT_0456 | Thioredoxin; Belongs to the thioredoxin family. | Chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.616 |
| LBAT_1627 | hslU | LBAT_1627 | LBAT_0916 | Thioredoxin; Belongs to the thioredoxin family. | 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. | 0.531 |
| LBAT_1627 | recA | LBAT_1627 | LBAT_1172 | Thioredoxin; Belongs to the thioredoxin family. | Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.513 |
| LBAT_1627 | trxB | LBAT_1627 | LBAT_1152 | Thioredoxin; Belongs to the thioredoxin family. | Thioredoxin reductase. | 0.789 |
| LBAT_1627 | tuf | LBAT_1627 | LBAT_0983 | Thioredoxin; Belongs to the thioredoxin family. | Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. | 0.531 |
| fusA | LBAT_1627 | LBAT_0353 | LBAT_1627 | 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. | 0.619 |
| 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. | 0.502 |
| 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. | 0.738 |
| fusA | recA | LBAT_0353 | LBAT_1172 | 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. | Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.658 |