| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CH53_431 | b4155 | CH53_431 | CH53_1352 | Hypothetical protein. | EF-P lysine aminoacylase GenX; 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. | 0.466 |
| CH53_431 | efp | CH53_431 | CH53_1361 | Hypothetical protein. | Translation 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; Belongs to the elongation factor P family. | 0.498 |
| CH53_431 | epmB | CH53_431 | CH53_1362 | Hypothetical protein. | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | 0.599 |
| atoD | epmB | CH53_2127 | CH53_1362 | Acetate CoA-transferase subunit alpha. | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | 0.420 |
| b4155 | CH53_431 | CH53_1352 | CH53_431 | EF-P lysine aminoacylase GenX; 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. | Hypothetical protein. | 0.466 |
| b4155 | efp | CH53_1352 | CH53_1361 | EF-P lysine aminoacylase GenX; 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. | Translation 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; Belongs to the elongation factor P family. | 0.903 |
| b4155 | epmB | CH53_1352 | CH53_1362 | EF-P lysine aminoacylase GenX; 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. | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | 0.847 |
| cheR | epmB | CH53_3540 | CH53_1362 | Chemotaxis protein methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | 0.790 |
| cheR | nifJ | CH53_3540 | CH53_4046 | Chemotaxis protein methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; pyruv_ox_red: pyruvate:ferredoxin (flavodoxin) oxidoreductase. | 0.939 |
| efp | CH53_431 | CH53_1361 | CH53_431 | Translation 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; Belongs to the elongation factor P family. | Hypothetical protein. | 0.498 |
| efp | b4155 | CH53_1361 | CH53_1352 | Translation 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; Belongs to the elongation factor P family. | EF-P lysine aminoacylase GenX; 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. | 0.903 |
| efp | epmB | CH53_1361 | CH53_1362 | Translation 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; Belongs to the elongation factor P family. | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | 0.858 |
| epmB | CH53_431 | CH53_1362 | CH53_431 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | Hypothetical protein. | 0.599 |
| epmB | atoD | CH53_1362 | CH53_2127 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | Acetate CoA-transferase subunit alpha. | 0.420 |
| epmB | b4155 | CH53_1362 | CH53_1352 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | EF-P lysine aminoacylase GenX; 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. | 0.847 |
| epmB | cheR | CH53_1362 | CH53_3540 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | Chemotaxis protein methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. | 0.790 |
| epmB | efp | CH53_1362 | CH53_1361 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | Translation 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; Belongs to the elongation factor P family. | 0.858 |
| epmB | nifJ | CH53_1362 | CH53_4046 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; pyruv_ox_red: pyruvate:ferredoxin (flavodoxin) oxidoreductase. | 0.631 |
| epmB | rnt | CH53_1362 | CH53_4094 | EFP_modif_epmB: EF-P beta-lysylation protein EpmB. | Ribonuclease T; Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis. | 0.402 |
| nifJ | cheR | CH53_4046 | CH53_3540 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; pyruv_ox_red: pyruvate:ferredoxin (flavodoxin) oxidoreductase. | Chemotaxis protein methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. | 0.939 |