node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PFL_0359 | mltF | PFL_0359 | PFL_1075 | Identified by match to protein family HMM PF05170. | 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. | 0.468 |
PFL_1077 | mltF | PFL_1077 | PFL_1075 | Conserved hypothetical protein. | 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. | 0.490 |
PFL_1077 | purL | PFL_1077 | PFL_1076 | Conserved hypothetical protein. | 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. | 0.832 |
PFL_1452 | mltF | PFL_1452 | PFL_1075 | Peptidase, M48 family; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. | 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. | 0.402 |
PFL_3300 | mltF | PFL_3300 | PFL_1075 | Putative membrane-bound lytic murein transglycosylase; Identified by similarity to SP:P23931; match to protein family HMM PF01464; match to protein family HMM PF01476; match to protein family HMM PF06474. | 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. | 0.538 |
PFL_3300 | rlpA-2 | PFL_3300 | PFL_5449 | Putative membrane-bound lytic murein transglycosylase; Identified by similarity to SP:P23931; match to protein family HMM PF01464; match to protein family HMM PF01476; match to protein family HMM PF06474. | Lipoprotein, RlpA family; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.575 |
mltF | PFL_0359 | PFL_1075 | PFL_0359 | 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. | Identified by match to protein family HMM PF05170. | 0.468 |
mltF | PFL_1077 | PFL_1075 | PFL_1077 | 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. | Conserved hypothetical protein. | 0.490 |
mltF | PFL_1452 | PFL_1075 | PFL_1452 | 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. | Peptidase, M48 family; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. | 0.402 |
mltF | PFL_3300 | PFL_1075 | PFL_3300 | 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. | Putative membrane-bound lytic murein transglycosylase; Identified by similarity to SP:P23931; match to protein family HMM PF01464; match to protein family HMM PF01476; match to protein family HMM PF06474. | 0.538 |
mltF | purL | PFL_1075 | PFL_1076 | 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. | 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. | 0.755 |
mltF | rlpA-2 | PFL_1075 | PFL_5449 | 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. | Lipoprotein, RlpA family; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.437 |
purL | PFL_1077 | PFL_1076 | PFL_1077 | 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. | Conserved hypothetical protein. | 0.832 |
purL | mltF | PFL_1076 | PFL_1075 | 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. | 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. | 0.755 |
rlpA-2 | PFL_3300 | PFL_5449 | PFL_3300 | Lipoprotein, RlpA family; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | Putative membrane-bound lytic murein transglycosylase; Identified by similarity to SP:P23931; match to protein family HMM PF01464; match to protein family HMM PF01476; match to protein family HMM PF06474. | 0.575 |
rlpA-2 | mltF | PFL_5449 | PFL_1075 | Lipoprotein, RlpA family; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 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. | 0.437 |