| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hslO | hslR | BAU10_15775 | BAU10_15780 | Hsp33 family molecular chaperone; 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; Belongs to the HSP15 family. | 0.983 |
| hslO | hslU | BAU10_15775 | BAU10_00280 | Hsp33 family molecular chaperone; 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. | HslU--HslV peptidase ATPase subunit; 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. | 0.861 |
| hslO | hslV | BAU10_15775 | BAU10_00285 | Hsp33 family molecular chaperone; 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. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.852 |
| hslR | hslO | BAU10_15780 | BAU10_15775 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Hsp33 family molecular chaperone; 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. | 0.983 |
| hslR | hslU | BAU10_15780 | BAU10_00280 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | HslU--HslV peptidase ATPase subunit; 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. | 0.846 |
| hslR | hslV | BAU10_15780 | BAU10_00285 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.842 |
| hslR | rplB | BAU10_15780 | BAU10_00330 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 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. | 0.807 |
| hslR | rplQ | BAU10_15780 | BAU10_00445 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 50S ribosomal protein L17; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.855 |
| hslR | rplS | BAU10_15780 | BAU10_12195 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 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. | 0.889 |
| hslR | rplY | BAU10_15780 | BAU10_05375 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 50S ribosomal protein L25; This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Belongs to the bacterial ribosomal protein bL25 family. | 0.792 |
| hslR | rpmA | BAU10_15780 | BAU10_00655 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 50S ribosomal protein L27; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL27 family. | 0.807 |
| hslR | rpmB | BAU10_15780 | BAU10_16045 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 50S ribosomal protein L28; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL28 family. | 0.814 |
| hslR | rpmH | BAU10_15780 | BAU10_15160 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 50S ribosomal protein L34; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL34 family. | 0.809 |
| hslU | hslO | BAU10_00280 | BAU10_15775 | HslU--HslV peptidase ATPase subunit; 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. | Hsp33 family molecular chaperone; 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. | 0.861 |
| hslU | hslR | BAU10_00280 | BAU10_15780 | HslU--HslV peptidase ATPase subunit; 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; Belongs to the HSP15 family. | 0.846 |
| hslU | hslV | BAU10_00280 | BAU10_00285 | HslU--HslV peptidase ATPase subunit; 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. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| hslV | hslO | BAU10_00285 | BAU10_15775 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Hsp33 family molecular chaperone; 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. | 0.852 |
| hslV | hslR | BAU10_00285 | BAU10_15780 | HslU--HslV peptidase proteolytic subunit; 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; Belongs to the HSP15 family. | 0.842 |
| hslV | hslU | BAU10_00285 | BAU10_00280 | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | HslU--HslV peptidase ATPase subunit; 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 | BAU10_00330 | BAU10_15780 | 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; Belongs to the HSP15 family. | 0.807 |
