| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANQ20877.1 | ANQ22854.1 | BA893_04060 | BA893_14840 | Chemotaxis protein CheR; Derived by automated computational analysis using gene prediction method: Protein Homology. | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.814 |
| ANQ22229.1 | ANQ22854.1 | BA893_11325 | BA893_14840 | Elongation factor P hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.604 |
| ANQ22229.1 | efp | BA893_11325 | BA893_14835 | Elongation factor P hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.497 |
| ANQ22229.1 | epmA | BA893_11325 | BA893_14805 | Elongation factor P hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Elongation factor P lysine(34) lysyltransferase; 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. | 0.512 |
| ANQ22854.1 | ANQ20877.1 | BA893_14840 | BA893_04060 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chemotaxis protein CheR; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.814 |
| ANQ22854.1 | ANQ22229.1 | BA893_14840 | BA893_11325 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Elongation factor P hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.604 |
| ANQ22854.1 | ANQ22855.1 | BA893_14840 | BA893_14845 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.556 |
| ANQ22854.1 | efp | BA893_14840 | BA893_14835 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.873 |
| ANQ22854.1 | epmA | BA893_14840 | BA893_14805 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Elongation factor P lysine(34) lysyltransferase; 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. | 0.831 |
| ANQ22854.1 | fadB | BA893_14840 | BA893_00090 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Multifunctional fatty acid oxidation complex subunit alpha; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.408 |
| ANQ22854.1 | fadJ | BA893_14840 | BA893_11365 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Multifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.408 |
| ANQ22854.1 | trpR | BA893_14840 | BA893_02775 | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Trp operon repressor; This protein is an aporepressor. When complexed with L- tryptophan it binds the operator region of the trp operon and prevents the initiation of transcription. | 0.402 |
| ANQ22855.1 | ANQ22854.1 | BA893_14845 | BA893_14840 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.556 |
| ANQ22855.1 | efp | BA893_14845 | BA893_14835 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.440 |
| efp | ANQ22229.1 | BA893_14835 | BA893_11325 | 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. | Elongation factor P hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.497 |
| efp | ANQ22854.1 | BA893_14835 | BA893_14840 | 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 beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.873 |
| efp | ANQ22855.1 | BA893_14835 | BA893_14845 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.440 |
| efp | epmA | BA893_14835 | BA893_14805 | 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. | Elongation factor P lysine(34) lysyltransferase; 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. | 0.920 |
| epmA | ANQ22229.1 | BA893_14805 | BA893_11325 | Elongation factor P lysine(34) lysyltransferase; 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 hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.512 |
| epmA | ANQ22854.1 | BA893_14805 | BA893_14840 | Elongation factor P lysine(34) lysyltransferase; 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. | EF-P beta-lysylation protein EpmB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.831 |