node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Spea_1224 | mltF | Spea_1224 | Spea_1316 | TIGRFAM: ribosomal subunit interface protein; PFAM: sigma 54 modulation protein/ribosomal protein S30EA; KEGG: slo:Shew_1241 sigma 54 modulation protein/ribosomal protein S30EA. | Lytic transglycosylase catalytic; 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. | 0.412 |
Spea_1224 | purL | Spea_1224 | Spea_1317 | TIGRFAM: ribosomal subunit interface protein; PFAM: sigma 54 modulation protein/ribosomal protein S30EA; KEGG: slo:Shew_1241 sigma 54 modulation protein/ribosomal protein S30EA. | 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. | 0.407 |
Spea_1455 | mltF | Spea_1455 | Spea_1316 | KEGG: slo:Shew_1448 hypothetical protein. | Lytic transglycosylase catalytic; 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. | 0.833 |
Spea_2407 | Spea_2415 | Spea_2407 | Spea_2415 | PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: slo:Shew_2115 lytic transglycosylase, catalytic. | PFAM: Lytic transglycosylase catalytic; KEGG: slo:Shew_2125 lytic transglycosylase, catalytic. | 0.551 |
Spea_2407 | mltF | Spea_2407 | Spea_1316 | PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: slo:Shew_2115 lytic transglycosylase, catalytic. | Lytic transglycosylase catalytic; 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. | 0.517 |
Spea_2415 | Spea_2407 | Spea_2415 | Spea_2407 | PFAM: Lytic transglycosylase catalytic; KEGG: slo:Shew_2125 lytic transglycosylase, catalytic. | PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: slo:Shew_2115 lytic transglycosylase, catalytic. | 0.551 |
Spea_2415 | mltF | Spea_2415 | Spea_1316 | PFAM: Lytic transglycosylase catalytic; KEGG: slo:Shew_2125 lytic transglycosylase, catalytic. | Lytic transglycosylase catalytic; 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. | 0.475 |
mltF | Spea_1224 | Spea_1316 | Spea_1224 | Lytic transglycosylase catalytic; 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. | TIGRFAM: ribosomal subunit interface protein; PFAM: sigma 54 modulation protein/ribosomal protein S30EA; KEGG: slo:Shew_1241 sigma 54 modulation protein/ribosomal protein S30EA. | 0.412 |
mltF | Spea_1455 | Spea_1316 | Spea_1455 | Lytic transglycosylase catalytic; 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. | KEGG: slo:Shew_1448 hypothetical protein. | 0.833 |
mltF | Spea_2407 | Spea_1316 | Spea_2407 | Lytic transglycosylase catalytic; 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. | PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: slo:Shew_2115 lytic transglycosylase, catalytic. | 0.517 |
mltF | Spea_2415 | Spea_1316 | Spea_2415 | Lytic transglycosylase catalytic; 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. | PFAM: Lytic transglycosylase catalytic; KEGG: slo:Shew_2125 lytic transglycosylase, catalytic. | 0.475 |
mltF | purL | Spea_1316 | Spea_1317 | Lytic transglycosylase catalytic; 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. | 0.743 |
mltF | rlpA | Spea_1316 | Spea_3152 | Lytic transglycosylase catalytic; 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. | 0.460 |
purL | Spea_1224 | Spea_1317 | Spea_1224 | 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. | TIGRFAM: ribosomal subunit interface protein; PFAM: sigma 54 modulation protein/ribosomal protein S30EA; KEGG: slo:Shew_1241 sigma 54 modulation protein/ribosomal protein S30EA. | 0.407 |
purL | mltF | Spea_1317 | Spea_1316 | 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. | Lytic transglycosylase catalytic; 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. | 0.743 |
rlpA | mltF | Spea_3152 | Spea_1316 | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | Lytic transglycosylase catalytic; 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. | 0.460 |