| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ31020.1 | EAQ31389.1 | OS145_10783 | OS145_04690 | COG0741 Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains). | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.532 |
| EAQ31386.1 | EAQ31389.1 | OS145_04675 | OS145_04690 | COG0046 Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain. | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.701 |
| EAQ31386.1 | EAQ31390.1 | OS145_04675 | OS145_04695 | COG0046 Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain. | COG1473 Metal-dependent amidase/aminoacylase/carboxypeptidase. | 0.479 |
| EAQ31389.1 | EAQ31020.1 | OS145_04690 | OS145_10783 | Predicted 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. In the N-terminal section; belongs to the ba [...] | COG0741 Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains). | 0.532 |
| EAQ31389.1 | EAQ31386.1 | OS145_04690 | OS145_04675 | Predicted 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. In the N-terminal section; belongs to the ba [...] | COG0046 Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain. | 0.701 |
| EAQ31389.1 | EAQ31390.1 | OS145_04690 | OS145_04695 | Predicted 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. In the N-terminal section; belongs to the ba [...] | COG1473 Metal-dependent amidase/aminoacylase/carboxypeptidase. | 0.830 |
| EAQ31389.1 | EAQ31391.1 | OS145_04690 | OS145_04700 | Predicted 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. In the N-terminal section; belongs to the ba [...] | COG0590 Cytosine/adenosine deaminases. | 0.803 |
| EAQ31389.1 | EAQ31630.1 | OS145_04690 | OS145_05285 | Predicted 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. In the N-terminal section; belongs to the ba [...] | COG3107 Putative lipoprotein. | 0.414 |
| EAQ31389.1 | EAQ33010.1 | OS145_04690 | OS145_04248 | Predicted 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. In the N-terminal section; belongs to the ba [...] | Hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. | 0.413 |
| EAQ31389.1 | EAQ33351.1 | OS145_04690 | OS145_03245 | Predicted 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. In the N-terminal section; belongs to the ba [...] | COG0741 Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains). | 0.400 |
| EAQ31390.1 | EAQ31386.1 | OS145_04695 | OS145_04675 | COG1473 Metal-dependent amidase/aminoacylase/carboxypeptidase. | COG0046 Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain. | 0.479 |
| EAQ31390.1 | EAQ31389.1 | OS145_04695 | OS145_04690 | COG1473 Metal-dependent amidase/aminoacylase/carboxypeptidase. | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.830 |
| EAQ31390.1 | EAQ31391.1 | OS145_04695 | OS145_04700 | COG1473 Metal-dependent amidase/aminoacylase/carboxypeptidase. | COG0590 Cytosine/adenosine deaminases. | 0.593 |
| EAQ31391.1 | EAQ31389.1 | OS145_04700 | OS145_04690 | COG0590 Cytosine/adenosine deaminases. | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.803 |
| EAQ31391.1 | EAQ31390.1 | OS145_04700 | OS145_04695 | COG0590 Cytosine/adenosine deaminases. | COG1473 Metal-dependent amidase/aminoacylase/carboxypeptidase. | 0.593 |
| EAQ31630.1 | EAQ31389.1 | OS145_05285 | OS145_04690 | COG3107 Putative lipoprotein. | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.414 |
| EAQ33010.1 | EAQ31389.1 | OS145_04248 | OS145_04690 | Hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.413 |
| EAQ33351.1 | EAQ31389.1 | OS145_03245 | OS145_04690 | COG0741 Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains). | Predicted 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. In the N-terminal section; belongs to the ba [...] | 0.400 |
