| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMB84010.1 | AMB86982.1 | AWM79_01275 | AWM79_17425 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.432 |
| AMB84010.1 | hslU | AWM79_01275 | AWM79_17420 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.887 |
| AMB84010.1 | hslV | AWM79_01275 | AWM79_17415 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.873 |
| AMB84010.1 | lon | AWM79_01275 | AWM79_09980 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.545 |
| AMB85568.1 | AMB86982.1 | AWM79_09770 | AWM79_17425 | ATP-binding protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.653 |
| AMB86982.1 | AMB84010.1 | AWM79_17425 | AWM79_01275 | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.432 |
| AMB86982.1 | AMB85568.1 | AWM79_17425 | AWM79_09770 | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-binding protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.653 |
| AMB86982.1 | hslU | AWM79_17425 | AWM79_17420 | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.729 |
| AMB86982.1 | hslV | AWM79_17425 | AWM79_17415 | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.671 |
| AMB86982.1 | lon | AWM79_17425 | AWM79_09980 | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.501 |
| AMB86982.1 | thrB | AWM79_17425 | AWM79_13125 | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pseudomonas-type ThrB family. | 0.531 |
| hslU | AMB84010.1 | AWM79_17420 | AWM79_01275 | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.887 |
| hslU | AMB86982.1 | AWM79_17420 | AWM79_17425 | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.729 |
| hslU | hslV | AWM79_17420 | AWM79_17415 | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| hslU | lon | AWM79_17420 | AWM79_09980 | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.826 |
| hslV | AMB84010.1 | AWM79_17415 | AWM79_01275 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.873 |
| hslV | AMB86982.1 | AWM79_17415 | AWM79_17425 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.671 |
| hslV | hslU | AWM79_17415 | AWM79_17420 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.999 |
| hslV | lon | AWM79_17415 | AWM79_09980 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.805 |
| lon | AMB84010.1 | AWM79_09980 | AWM79_01275 | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.545 |
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