| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0116 | PP_4785 | PP_0116 | PP_4785 | Putative lipoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. | Homologs of previously reported genes of unknown function. | 0.584 |
| PP_0116 | mltF | PP_0116 | PP_1036 | Putative lipoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.550 |
| PP_0287 | PP_2130 | PP_0287 | PP_2130 | Homologs of previously reported genes of unknown function. | Putative Soluble lytic transglycosylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.898 |
| PP_0287 | mltF | PP_0287 | PP_1036 | Homologs of previously reported genes of unknown function. | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.478 |
| PP_1038 | mltF | PP_1038 | PP_1036 | Homologs of previously reported genes of unknown function. | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.488 |
| PP_1038 | purL | PP_1038 | PP_1037 | Homologs of previously reported genes of unknown function. | 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. | 0.875 |
| PP_2130 | PP_0287 | PP_2130 | PP_0287 | Putative Soluble lytic transglycosylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Homologs of previously reported genes of unknown function. | 0.898 |
| PP_2130 | mltF | PP_2130 | PP_1036 | Putative Soluble lytic transglycosylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.472 |
| PP_2130 | yceG | PP_2130 | PP_1918 | Putative Soluble lytic transglycosylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Septation protein; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. | 0.895 |
| PP_4785 | PP_0116 | PP_4785 | PP_0116 | Homologs of previously reported genes of unknown function. | Putative lipoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. | 0.584 |
| PP_4785 | mltF | PP_4785 | PP_1036 | Homologs of previously reported genes of unknown function. | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.575 |
| mltB | mltD | PP_4805 | PP_4145 | Membrane-bound lytic murein transglycosylase B; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Cellenvelope : Biosynthesis and degradation of murein sacculus and peptidoglycan. | Membrane-bound lytic murein transglycosylase D. | 0.584 |
| mltB | mltF | PP_4805 | PP_1036 | Membrane-bound lytic murein transglycosylase B; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Cellenvelope : Biosynthesis and degradation of murein sacculus and peptidoglycan. | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.598 |
| mltB | rlpA-2 | PP_4805 | PP_0929 | Membrane-bound lytic murein transglycosylase B; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Cellenvelope : Biosynthesis and degradation of murein sacculus and peptidoglycan. | Putative Lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.617 |
| mltB | yceG | PP_4805 | PP_1918 | Membrane-bound lytic murein transglycosylase B; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Cellenvelope : Biosynthesis and degradation of murein sacculus and peptidoglycan. | Septation protein; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. | 0.472 |
| mltD | mltB | PP_4145 | PP_4805 | Membrane-bound lytic murein transglycosylase D. | Membrane-bound lytic murein transglycosylase B; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Cellenvelope : Biosynthesis and degradation of murein sacculus and peptidoglycan. | 0.584 |
| mltD | mltF | PP_4145 | PP_1036 | 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. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.721 |
| mltD | purL | PP_4145 | PP_1037 | Membrane-bound lytic murein transglycosylase D. | 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. | 0.413 |
| mltD | rlpA-2 | PP_4145 | PP_0929 | Membrane-bound lytic murein transglycosylase D. | Putative Lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.658 |
| mltD | yceG | PP_4145 | PP_1918 | Membrane-bound lytic murein transglycosylase D. | Septation protein; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. | 0.680 |