node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFU29227.1 | SFU62203.1 | SAMN05421784_10293 | SAMN05421784_11552 | Flagellar protein FlgJ. | Membrane-bound lytic murein transglycosylase D. | 0.430 |
SFU29227.1 | mltF | SAMN05421784_10293 | SAMN05421784_10137 | Flagellar protein FlgJ. | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.450 |
SFU62158.1 | SFU62203.1 | SAMN05421784_11550 | SAMN05421784_11552 | Methyltransferase domain-containing protein. | Membrane-bound lytic murein transglycosylase D. | 0.608 |
SFU62158.1 | mltF | SAMN05421784_11550 | SAMN05421784_10137 | Methyltransferase domain-containing protein. | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.443 |
SFU62203.1 | SFU29227.1 | SAMN05421784_11552 | SAMN05421784_10293 | Membrane-bound lytic murein transglycosylase D. | Flagellar protein FlgJ. | 0.430 |
SFU62203.1 | SFU62158.1 | SAMN05421784_11552 | SAMN05421784_11550 | Membrane-bound lytic murein transglycosylase D. | Methyltransferase domain-containing protein. | 0.608 |
SFU62203.1 | mltF | SAMN05421784_11552 | SAMN05421784_10137 | Membrane-bound lytic murein transglycosylase D. | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.556 |
lolB | mltF | SAMN05421784_10343 | SAMN05421784_10137 | Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.434 |
mltF | SFU29227.1 | SAMN05421784_10137 | SAMN05421784_10293 | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | Flagellar protein FlgJ. | 0.450 |
mltF | SFU62158.1 | SAMN05421784_10137 | SAMN05421784_11550 | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | Methyltransferase domain-containing protein. | 0.443 |
mltF | SFU62203.1 | SAMN05421784_10137 | SAMN05421784_11552 | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | Membrane-bound lytic murein transglycosylase D. | 0.556 |
mltF | lolB | SAMN05421784_10137 | SAMN05421784_10343 | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | Outer membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.434 |
mltF | nadE | SAMN05421784_10137 | SAMN05421784_10131 | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | NAD+ synthase (glutamine-hydrolysing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.411 |
mltF | purL | SAMN05421784_10137 | SAMN05421784_10136 | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.650 |
nadE | mltF | SAMN05421784_10131 | SAMN05421784_10137 | NAD+ synthase (glutamine-hydrolysing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.411 |
nadE | purL | SAMN05421784_10131 | SAMN05421784_10136 | NAD+ synthase (glutamine-hydrolysing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.676 |
purL | mltF | SAMN05421784_10136 | SAMN05421784_10137 | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | Membrane-bound lytic murein transglycosylase F; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. | 0.650 |
purL | nadE | SAMN05421784_10136 | SAMN05421784_10131 | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | NAD+ synthase (glutamine-hydrolysing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.676 |