| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| THII_0940 | mltF | THII_0940 | THII_2610 | LysM repeat-containing protein. | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | 0.431 |
| THII_0940 | purL | THII_0940 | THII_3019 | LysM repeat-containing protein. | Phosphoribosylformylglycinamidine synthase, single chain form; 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. | 0.639 |
| THII_2056 | mltF | THII_2056 | THII_2610 | Lytic murein transglycosylase. | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | 0.481 |
| adk | mltF | THII_2611 | THII_2610 | Adenylate kinase family protein; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | 0.493 |
| mltF | THII_0940 | THII_2610 | THII_0940 | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | LysM repeat-containing protein. | 0.431 |
| mltF | THII_2056 | THII_2610 | THII_2056 | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | Lytic murein transglycosylase. | 0.481 |
| mltF | adk | THII_2610 | THII_2611 | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | Adenylate kinase family protein; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. | 0.493 |
| mltF | nudJ | THII_2610 | THII_2717 | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. NudJ subfamily. | 0.456 |
| mltF | purL | THII_2610 | THII_3019 | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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, single chain form; 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. | 0.507 |
| nudJ | mltF | THII_2717 | THII_2610 | ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. NudJ subfamily. | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | 0.456 |
| purL | THII_0940 | THII_3019 | THII_0940 | Phosphoribosylformylglycinamidine synthase, single chain form; 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. | LysM repeat-containing protein. | 0.639 |
| purL | mltF | THII_3019 | THII_2610 | Phosphoribosylformylglycinamidine synthase, single chain form; 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. | Putative soluble lytic transglycosylase fused to an ABC-type amino acid-binding protein; 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. | 0.507 |