| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aroC | mepA | STM2384 | STM2383 | 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 DD-endopeptidase; 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. Belongs to the peptidase M74 family. | 0.912 |
| aroC | yfcA | STM2384 | STM2382 | 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. | Similar to E. coli putative structural protein (AAC75387.1); Blastp hit to AAC75387.1 (269 aa), 90% identity in aa 1 - 269. | 0.825 |
| aroC | yfcB | STM2384 | STM2385 | 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. | Putative methylase; Specifically methylates the 50S ribosomal protein L3 on 'Gln- 150'; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. | 0.933 |
| aroC | yfcL | STM2384 | STM2380 | 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. | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC75385.1); Blastp hit to AAC75385.1 (92 aa), 85% identity in aa 1 - 91. | 0.780 |
| aroC | yfcM | STM2384 | STM2381 | 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. | Putative cytoplasmic protein; Similar to E. coli putative transporting ATPase (AAC75386.1); Blastp hit to AAC75386.1 (182 aa), 92% identity in aa 1 - 182. | 0.824 |
| aroC | yfcN | STM2384 | STM2386 | 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. | Putative Smr domain containing protein; Similar to E. coli orf, hypothetical protein (AAC75391.1); Blastp hit to AAC75391.1 (183 aa), 93% identity in aa 1 - 183; Belongs to the UPF0115 family. | 0.544 |
| efp | yfcM | STM4334 | STM2381 | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. | Putative cytoplasmic protein; Similar to E. coli putative transporting ATPase (AAC75386.1); Blastp hit to AAC75386.1 (182 aa), 92% identity in aa 1 - 182. | 0.939 |
| efp | yjeA | STM4334 | STM4344 | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. | Putative pyruvate oxidase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta- lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF- P 'Lys-34' (Probable). Can also use L-alpha-lysine as a substrate, but probably with lower efficiency. Cannot aminoacylate tRNA(Lys) with lysine. | 0.989 |
| efp | yjeK | STM4334 | STM4333 | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. | Putative aminomutase; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3- aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity). | 0.994 |
| mepA | aroC | STM2383 | STM2384 | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | 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. | 0.912 |
| mepA | yfcA | STM2383 | STM2382 | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | Similar to E. coli putative structural protein (AAC75387.1); Blastp hit to AAC75387.1 (269 aa), 90% identity in aa 1 - 269. | 0.957 |
| mepA | yfcB | STM2383 | STM2385 | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | Putative methylase; Specifically methylates the 50S ribosomal protein L3 on 'Gln- 150'; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. | 0.922 |
| mepA | yfcL | STM2383 | STM2380 | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC75385.1); Blastp hit to AAC75385.1 (92 aa), 85% identity in aa 1 - 91. | 0.780 |
| mepA | yfcM | STM2383 | STM2381 | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | Putative cytoplasmic protein; Similar to E. coli putative transporting ATPase (AAC75386.1); Blastp hit to AAC75386.1 (182 aa), 92% identity in aa 1 - 182. | 0.839 |
| mepA | yfcN | STM2383 | STM2386 | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | Putative Smr domain containing protein; Similar to E. coli orf, hypothetical protein (AAC75391.1); Blastp hit to AAC75391.1 (183 aa), 93% identity in aa 1 - 183; Belongs to the UPF0115 family. | 0.499 |
| yeiP | yfcM | STM2211 | STM2381 | Similar to E. coli putative elongation factor (AAC75232.1); Blastp hit to AAC75232.1 (275 aa), 83% identity in aa 8 - 275. | Putative cytoplasmic protein; Similar to E. coli putative transporting ATPase (AAC75386.1); Blastp hit to AAC75386.1 (182 aa), 92% identity in aa 1 - 182. | 0.915 |
| yeiP | yjeA | STM2211 | STM4344 | Similar to E. coli putative elongation factor (AAC75232.1); Blastp hit to AAC75232.1 (275 aa), 83% identity in aa 8 - 275. | Putative pyruvate oxidase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta- lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF- P 'Lys-34' (Probable). Can also use L-alpha-lysine as a substrate, but probably with lower efficiency. Cannot aminoacylate tRNA(Lys) with lysine. | 0.973 |
| yeiP | yjeK | STM2211 | STM4333 | Similar to E. coli putative elongation factor (AAC75232.1); Blastp hit to AAC75232.1 (275 aa), 83% identity in aa 8 - 275. | Putative aminomutase; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3- aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity). | 0.962 |
| yfcA | aroC | STM2382 | STM2384 | Similar to E. coli putative structural protein (AAC75387.1); Blastp hit to AAC75387.1 (269 aa), 90% identity in aa 1 - 269. | 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 |
| yfcA | mepA | STM2382 | STM2383 | Similar to E. coli putative structural protein (AAC75387.1); Blastp hit to AAC75387.1 (269 aa), 90% identity in aa 1 - 269. | Penicillin-insensitive murein DD-endopeptidase; 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. Belongs to the peptidase M74 family. | 0.957 |
