| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa0986 | efp | PSHAa0986 | PSHAa0474 | Homologs of previously reported genes of unknown function. | Elongation factor P (EF-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; Belongs to the elongation factor P family. | 0.567 |
| PSHAa0986 | epmA | PSHAa0986 | PSHAa0475 | Homologs of previously reported genes of unknown function. | Putative fold recognizing lysyl-tRNA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). 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 a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | 0.500 |
| PSHAa0986 | kamA | PSHAa0986 | PSHAa0473 | Homologs of previously reported genes of unknown function. | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.709 |
| cheR | kamA | PSHAa0767 | PSHAa0473 | Chemotaxis protein methyltransferase CheR; Function of homologous gene experimentally demonstrated in an other organism; regulator. | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.792 |
| efp | PSHAa0986 | PSHAa0474 | PSHAa0986 | Elongation factor P (EF-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; Belongs to the elongation factor P family. | Homologs of previously reported genes of unknown function. | 0.567 |
| efp | epmA | PSHAa0474 | PSHAa0475 | Elongation factor P (EF-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; Belongs to the elongation factor P family. | Putative fold recognizing lysyl-tRNA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). 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 a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | 0.974 |
| efp | kamA | PSHAa0474 | PSHAa0473 | Elongation factor P (EF-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; Belongs to the elongation factor P family. | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.930 |
| epmA | PSHAa0986 | PSHAa0475 | PSHAa0986 | Putative fold recognizing lysyl-tRNA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). 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 a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | Homologs of previously reported genes of unknown function. | 0.500 |
| epmA | efp | PSHAa0475 | PSHAa0474 | Putative fold recognizing lysyl-tRNA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). 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 a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | Elongation factor P (EF-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; Belongs to the elongation factor P family. | 0.974 |
| epmA | kamA | PSHAa0475 | PSHAa0473 | Putative fold recognizing lysyl-tRNA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). 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 a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.960 |
| kamA | PSHAa0986 | PSHAa0473 | PSHAa0986 | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Homologs of previously reported genes of unknown function. | 0.709 |
| kamA | cheR | PSHAa0473 | PSHAa0767 | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Chemotaxis protein methyltransferase CheR; Function of homologous gene experimentally demonstrated in an other organism; regulator. | 0.792 |
| kamA | efp | PSHAa0473 | PSHAa0474 | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Elongation factor P (EF-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; Belongs to the elongation factor P family. | 0.930 |
| kamA | epmA | PSHAa0473 | PSHAa0475 | Putative lysine 2,3 aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Putative fold recognizing lysyl-tRNA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). 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 a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | 0.960 |
