| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hslO | hslR | AL538_10240 | AL538_10245 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.984 |
| hslO | hslU | AL538_10240 | AL538_10790 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 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. | 0.860 |
| hslO | hslV | AL538_10240 | AL538_10795 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.849 |
| hslR | hslO | AL538_10245 | AL538_10240 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.984 |
| hslR | hslU | AL538_10245 | AL538_10790 | Heat-shock protein; 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. | 0.845 |
| hslR | hslV | AL538_10245 | AL538_10795 | Heat-shock protein; 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. | 0.843 |
| hslR | rplB | AL538_10245 | AL538_10840 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. | 0.846 |
| hslR | rplQ | AL538_10245 | AL538_10955 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L17; Is a component of the macrolide binding site in the peptidyl transferase center; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.880 |
| hslR | rplS | AL538_10245 | AL538_06540 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | 0.911 |
| hslR | rplT | AL538_10245 | AL538_02115 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | 0.830 |
| hslR | rpmA | AL538_10245 | AL538_11160 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L27; Involved in the peptidyltransferase reaction during translation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL27 family. | 0.847 |
| hslR | rpmB | AL538_10245 | AL538_10525 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L28; Required for 70S ribosome assembly; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL28 family. | 0.848 |
| hslR | rpmH | AL538_10245 | AL538_09670 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L34; In Escherichia coli transcription of this gene is enhanced by polyamines; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL34 family. | 0.844 |
| hslU | hslO | AL538_10790 | AL538_10240 | 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. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.860 |
| hslU | hslR | AL538_10790 | AL538_10245 | 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. | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.845 |
| hslU | hslV | AL538_10790 | AL538_10795 | 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 |
| hslV | hslO | AL538_10795 | AL538_10240 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.849 |
| hslV | hslR | AL538_10795 | AL538_10245 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.843 |
| hslV | hslU | AL538_10795 | AL538_10790 | 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 |
| rplB | hslR | AL538_10840 | AL538_10245 | 50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.846 |
