| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALP39736.1 | ALP42799.1 | WL1483_4393 | WL1483_3380 | Putative DMT domain-containing membrane protein. | Hypothetical protein. | 0.583 |
| ALP39736.1 | ALP42948.1 | WL1483_4393 | WL1483_3529 | Putative DMT domain-containing membrane protein. | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.470 |
| ALP39736.1 | ALP43294.1 | WL1483_4393 | WL1483_3875 | Putative DMT domain-containing membrane protein. | Cytosolic long-chain acyl-CoA thioester hydrolase family protein. | 0.773 |
| ALP39736.1 | WL1483_69 | WL1483_4393 | WL1483_69 | Putative DMT domain-containing membrane protein. | Hypothetical protein. | 0.773 |
| ALP42799.1 | ALP39736.1 | WL1483_3380 | WL1483_4393 | Hypothetical protein. | Putative DMT domain-containing membrane protein. | 0.583 |
| ALP42799.1 | ALP42948.1 | WL1483_3380 | WL1483_3529 | Hypothetical protein. | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.613 |
| ALP42799.1 | ALP43294.1 | WL1483_3380 | WL1483_3875 | Hypothetical protein. | Cytosolic long-chain acyl-CoA thioester hydrolase family protein. | 0.584 |
| ALP42799.1 | WL1483_69 | WL1483_3380 | WL1483_69 | Hypothetical protein. | Hypothetical protein. | 0.583 |
| ALP42948.1 | ALP39736.1 | WL1483_3529 | WL1483_4393 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Putative DMT domain-containing membrane protein. | 0.470 |
| ALP42948.1 | ALP42799.1 | WL1483_3529 | WL1483_3380 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Hypothetical protein. | 0.613 |
| ALP42948.1 | ALP43294.1 | WL1483_3529 | WL1483_3875 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Cytosolic long-chain acyl-CoA thioester hydrolase family protein. | 0.471 |
| ALP42948.1 | WL1483_69 | WL1483_3529 | WL1483_69 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Hypothetical protein. | 0.470 |
| ALP42948.1 | mltC | WL1483_3529 | WL1483_4153 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Murein transglycosylase; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | 0.470 |
| ALP42948.1 | mltD | WL1483_3529 | WL1483_672 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Lytic transglycosylase. | 0.469 |
| ALP42948.1 | purL | WL1483_3529 | WL1483_961 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 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. | 0.465 |
| ALP42948.1 | yjbJ | WL1483_3529 | WL1483_1802 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Lytic transglycosylase, catalytic. | 0.469 |
| ALP42948.1 | yjbJ-2 | WL1483_3529 | WL1483_2880 | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Transglycosylase. | 0.487 |
| ALP43294.1 | ALP39736.1 | WL1483_3875 | WL1483_4393 | Cytosolic long-chain acyl-CoA thioester hydrolase family protein. | Putative DMT domain-containing membrane protein. | 0.773 |
| ALP43294.1 | ALP42799.1 | WL1483_3875 | WL1483_3380 | Cytosolic long-chain acyl-CoA thioester hydrolase family protein. | Hypothetical protein. | 0.584 |
| ALP43294.1 | ALP42948.1 | WL1483_3875 | WL1483_3529 | Cytosolic long-chain acyl-CoA thioester hydrolase family protein. | Lytic transglycosylase; 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.471 |
