node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OOC09455.1 | OOC10893.1 | B1A74_11230 | B1A74_03435 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lytic 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. | 0.456 |
OOC09455.1 | OOC10989.1 | B1A74_11230 | B1A74_02330 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.898 |
OOC10893.1 | OOC09455.1 | B1A74_03435 | B1A74_11230 | Lytic 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. | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.456 |
OOC10893.1 | OOC10894.1 | B1A74_03435 | B1A74_03440 | Lytic 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.588 |
OOC10893.1 | OOC10895.1 | B1A74_03435 | B1A74_03445 | Lytic 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. | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids; Belongs to the Maf family. YceF subfamily. | 0.501 |
OOC10893.1 | OOC10896.1 | B1A74_03435 | B1A74_03450 | Lytic 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. | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.436 |
OOC10893.1 | OOC10989.1 | B1A74_03435 | B1A74_02330 | Lytic 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. | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.556 |
OOC10893.1 | purL | B1A74_03435 | B1A74_00775 | Lytic 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. | 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. | 0.633 |
OOC10894.1 | OOC10893.1 | B1A74_03440 | B1A74_03435 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lytic 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. | 0.588 |
OOC10894.1 | OOC10895.1 | B1A74_03440 | B1A74_03445 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids; Belongs to the Maf family. YceF subfamily. | 0.559 |
OOC10894.1 | OOC10896.1 | B1A74_03440 | B1A74_03450 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.559 |
OOC10895.1 | OOC10893.1 | B1A74_03445 | B1A74_03435 | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids; Belongs to the Maf family. YceF subfamily. | Lytic 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. | 0.501 |
OOC10895.1 | OOC10894.1 | B1A74_03445 | B1A74_03440 | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids; Belongs to the Maf family. YceF subfamily. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.559 |
OOC10895.1 | OOC10896.1 | B1A74_03445 | B1A74_03450 | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids; Belongs to the Maf family. YceF subfamily. | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.832 |
OOC10896.1 | OOC10893.1 | B1A74_03450 | B1A74_03435 | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lytic 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. | 0.436 |
OOC10896.1 | OOC10894.1 | B1A74_03450 | B1A74_03440 | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.559 |
OOC10896.1 | OOC10895.1 | B1A74_03450 | B1A74_03445 | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | Septum formation inhibitor Maf; Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids; Belongs to the Maf family. YceF subfamily. | 0.832 |
OOC10896.1 | purL | B1A74_03450 | B1A74_00775 | Oxaloacetate decarboxylase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.533 |
OOC10989.1 | OOC09455.1 | B1A74_02330 | B1A74_11230 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.898 |
OOC10989.1 | OOC10893.1 | B1A74_02330 | B1A74_03435 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lytic 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. | 0.556 |