| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gntT | prlC | AB185_08650 | AB185_08655 | Gluconate transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.439 |
| gntT | rsmJ | AB185_08650 | AB185_08660 | Gluconate transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Methyltransferase; Specifically methylates the guanosine in position 1516 of 16S rRNA. | 0.439 |
| groEL | groES | AB185_33910 | AB185_33915 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
| groEL | grpE | AB185_33910 | AB185_14225 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | 0.988 |
| groEL | hslO | AB185_33910 | AB185_09100 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Hsp33-like chaperonin; 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. | 0.586 |
| groEL | htpG | AB185_33910 | AB185_29230 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.977 |
| groEL | ppiB | AB185_33910 | AB185_29005 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.459 |
| groEL | prlC | AB185_33910 | AB185_08655 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.454 |
| groEL | ybbN | AB185_33910 | AB185_29155 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.878 |
| groES | groEL | AB185_33915 | AB185_33910 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| groES | grpE | AB185_33915 | AB185_14225 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | 0.980 |
| groES | hslO | AB185_33915 | AB185_09100 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Hsp33-like chaperonin; 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. | 0.401 |
| groES | htpG | AB185_33915 | AB185_29230 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.880 |
| groES | ppiB | AB185_33915 | AB185_29005 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.725 |
| groES | prlC | AB185_33915 | AB185_08655 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.431 |
| groES | ybbN | AB185_33915 | AB185_29155 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.591 |
| grpE | groEL | AB185_14225 | AB185_33910 | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.988 |
| grpE | groES | AB185_14225 | AB185_33915 | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.980 |
| grpE | hslO | AB185_14225 | AB185_09100 | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | Hsp33-like chaperonin; 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. | 0.692 |
| grpE | htpG | AB185_14225 | AB185_29230 | Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...] | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.875 |
