| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CH53_1089 | mepA | CH53_1089 | CH53_433 | creA family protein. | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | 0.473 |
| CH53_136 | CH53_137 | CH53_136 | CH53_137 | Hypothetical protein. | L,D-transpeptidase catalytic domain protein. | 0.871 |
| CH53_136 | mepA | CH53_136 | CH53_433 | Hypothetical protein. | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | 0.704 |
| CH53_136 | ycjX | CH53_136 | CH53_4057 | Hypothetical protein. | Hypothetical protein. | 0.438 |
| CH53_137 | CH53_136 | CH53_137 | CH53_136 | L,D-transpeptidase catalytic domain protein. | Hypothetical protein. | 0.871 |
| CH53_137 | mepA | CH53_137 | CH53_433 | L,D-transpeptidase catalytic domain protein. | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | 0.455 |
| CH53_431 | aroC | CH53_431 | CH53_434 | Hypothetical protein. | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.639 |
| CH53_431 | mepA | CH53_431 | CH53_433 | Hypothetical protein. | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | 0.639 |
| CH53_431 | prmB | CH53_431 | CH53_435 | Hypothetical protein. | (glutamine-N5) methyltransferase, ribosomal protein L3-specific; Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. | 0.563 |
| CH53_431 | yfcA | CH53_431 | CH53_432 | Hypothetical protein. | Hypothetical protein. | 0.764 |
| aroC | CH53_431 | CH53_434 | CH53_431 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Hypothetical protein. | 0.639 |
| aroC | mepA | CH53_434 | CH53_433 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | 0.825 |
| aroC | prmB | CH53_434 | CH53_435 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | (glutamine-N5) methyltransferase, ribosomal protein L3-specific; Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. | 0.703 |
| aroC | yfcA | CH53_434 | CH53_432 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Hypothetical protein. | 0.809 |
| mepA | CH53_1089 | CH53_433 | CH53_1089 | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | creA family protein. | 0.473 |
| mepA | CH53_136 | CH53_433 | CH53_136 | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | Hypothetical protein. | 0.704 |
| mepA | CH53_137 | CH53_433 | CH53_137 | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | L,D-transpeptidase catalytic domain protein. | 0.455 |
| mepA | CH53_431 | CH53_433 | CH53_431 | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | Hypothetical protein. | 0.639 |
| mepA | aroC | CH53_433 | CH53_434 | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.825 |
| mepA | pldB | CH53_433 | CH53_2012 | Penicillin-insensitive murein endopeptidase family protein; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | Prolyl oligopeptidase family protein. | 0.550 |