node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDU83116.1 | SDU99165.1 | SAMN05216202_0234 | SAMN05216202_2786 | poly(beta-D-mannuronate) C5 epimerase. | Membrane-bound lytic murein transglycosylase MltF; 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. | 0.407 |
SDU83116.1 | SDV02722.1 | SAMN05216202_0234 | SAMN05216202_3372 | poly(beta-D-mannuronate) C5 epimerase. | Beta-galactosidase. | 0.772 |
SDU83116.1 | SDV07072.1 | SAMN05216202_0234 | SAMN05216202_4246 | poly(beta-D-mannuronate) C5 epimerase. | Hypothetical protein. | 0.703 |
SDU90704.1 | SDU99165.1 | SAMN05216202_1416 | SAMN05216202_2786 | Peptidyl-prolyl cis-trans isomerase D. | Membrane-bound lytic murein transglycosylase MltF; 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. | 0.427 |
SDU93546.1 | SDU99165.1 | SAMN05216202_1878 | SAMN05216202_2786 | Membrane-bound lytic murein transglycosylase D. | Membrane-bound lytic murein transglycosylase MltF; 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. | 0.617 |
SDU93546.1 | rlpA-2 | SAMN05216202_1878 | SAMN05216202_5425 | Membrane-bound lytic murein transglycosylase D. | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.590 |
SDU99158.1 | SDU99165.1 | SAMN05216202_2785 | SAMN05216202_2786 | Putative oxidoreductase. | Membrane-bound lytic murein transglycosylase MltF; 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 |
SDU99158.1 | SDU99173.1 | SAMN05216202_2785 | SAMN05216202_2787 | Putative oxidoreductase. | Sec-independent protein translocase TatD. | 0.441 |
SDU99165.1 | SDU83116.1 | SAMN05216202_2786 | SAMN05216202_0234 | Membrane-bound lytic murein transglycosylase MltF; 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. | poly(beta-D-mannuronate) C5 epimerase. | 0.407 |
SDU99165.1 | SDU90704.1 | SAMN05216202_2786 | SAMN05216202_1416 | Membrane-bound lytic murein transglycosylase MltF; 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. | Peptidyl-prolyl cis-trans isomerase D. | 0.427 |
SDU99165.1 | SDU93546.1 | SAMN05216202_2786 | SAMN05216202_1878 | Membrane-bound lytic murein transglycosylase MltF; 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. | Membrane-bound lytic murein transglycosylase D. | 0.617 |
SDU99165.1 | SDU99158.1 | SAMN05216202_2786 | SAMN05216202_2785 | Membrane-bound lytic murein transglycosylase MltF; 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 oxidoreductase. | 0.598 |
SDU99165.1 | SDU99173.1 | SAMN05216202_2786 | SAMN05216202_2787 | Membrane-bound lytic murein transglycosylase MltF; 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. | Sec-independent protein translocase TatD. | 0.610 |
SDU99165.1 | SDU99180.1 | SAMN05216202_2786 | SAMN05216202_2788 | Membrane-bound lytic murein transglycosylase MltF; 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. | Methyl-accepting chemotaxis protein. | 0.509 |
SDU99165.1 | SDV02722.1 | SAMN05216202_2786 | SAMN05216202_3372 | Membrane-bound lytic murein transglycosylase MltF; 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. | Beta-galactosidase. | 0.412 |
SDU99165.1 | SDV07072.1 | SAMN05216202_2786 | SAMN05216202_4246 | Membrane-bound lytic murein transglycosylase MltF; 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. | 0.472 |
SDU99165.1 | purL | SAMN05216202_2786 | SAMN05216202_3511 | Membrane-bound lytic murein transglycosylase MltF; 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. | 0.540 |
SDU99165.1 | rlpA-2 | SAMN05216202_2786 | SAMN05216202_5425 | Membrane-bound lytic murein transglycosylase MltF; 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. | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.451 |
SDU99173.1 | SDU99158.1 | SAMN05216202_2787 | SAMN05216202_2785 | Sec-independent protein translocase TatD. | Putative oxidoreductase. | 0.441 |
SDU99173.1 | SDU99165.1 | SAMN05216202_2787 | SAMN05216202_2786 | Sec-independent protein translocase TatD. | Membrane-bound lytic murein transglycosylase MltF; 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. | 0.610 |