| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| TM_1390 | TM_1391 | TM_1390 | TM_1391 | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | 0.553 |
| TM_1390 | TM_1392 | TM_1390 | TM_1392 | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | Hypothetical protein; Identified by sequence similarity; putative. | 0.553 |
| TM_1390 | hslO | TM_1390 | TM_1394 | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.564 |
| TM_1390 | ispD | TM_1390 | TM_1393 | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | 0.556 |
| TM_1391 | TM_1390 | TM_1391 | TM_1390 | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | 0.553 |
| TM_1391 | TM_1392 | TM_1391 | TM_1392 | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | Hypothetical protein; Identified by sequence similarity; putative. | 0.783 |
| TM_1391 | hslO | TM_1391 | TM_1394 | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.827 |
| TM_1391 | ispD | TM_1391 | TM_1393 | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | 0.792 |
| TM_1392 | TM_1390 | TM_1392 | TM_1390 | Hypothetical protein; Identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | 0.553 |
| TM_1392 | TM_1391 | TM_1392 | TM_1391 | Hypothetical protein; Identified by sequence similarity; putative. | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | 0.783 |
| TM_1392 | hslO | TM_1392 | TM_1394 | Hypothetical protein; Identified by sequence similarity; putative. | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.783 |
| TM_1392 | ispD | TM_1392 | TM_1393 | Hypothetical protein; Identified by sequence similarity; putative. | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | 0.783 |
| hslO | TM_1390 | TM_1394 | TM_1390 | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | 0.564 |
| hslO | TM_1391 | TM_1394 | TM_1391 | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | 0.827 |
| hslO | TM_1392 | TM_1394 | TM_1392 | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Hypothetical protein; Identified by sequence similarity; putative. | 0.783 |
| hslO | ispD | TM_1394 | TM_1393 | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | 0.810 |
| ispD | TM_1390 | TM_1393 | TM_1390 | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 50.00; identified by sequence similarity; putative. | 0.556 |
| ispD | TM_1391 | TM_1393 | TM_1391 | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | ATP-dependent Clp protease, ATPase subunit; Similar to PID:1001492 percent identity: 73.97; identified by sequence similarity; putative; Belongs to the ClpA/ClpB family. | 0.792 |
| ispD | TM_1392 | TM_1393 | TM_1392 | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | Hypothetical protein; Identified by sequence similarity; putative. | 0.783 |
| ispD | hslO | TM_1393 | TM_1394 | Conserved hypothetical protein; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | Conserved hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.810 |