| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ldb0672 | Ldb0674 | Ldb0672 | Ldb0674 | Amino-acid transporter. | Putative esterase (alpha-beta hydrolase superfamily). | 0.424 |
| Ldb0672 | msrA | Ldb0672 | Ldb0673 | Amino-acid transporter. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.446 |
| Ldb0674 | Ldb0672 | Ldb0674 | Ldb0672 | Putative esterase (alpha-beta hydrolase superfamily). | Amino-acid transporter. | 0.424 |
| Ldb0674 | msrA | Ldb0674 | Ldb0673 | Putative esterase (alpha-beta hydrolase superfamily). | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.733 |
| gidB | msrA | Ldb2056 | Ldb0673 | Methyltransferase GidB (Glucose inhibited division protein B); Specifically methylates the N7 position of a guanine in 16S rRNA; Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.567 |
| gidB | polA | Ldb2056 | Ldb1512 | Methyltransferase GidB (Glucose inhibited division protein B); Specifically methylates the N7 position of a guanine in 16S rRNA; Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.517 |
| groEL | groES | Ldb1617 | Ldb1618 | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
| groEL | hslO | Ldb1617 | Ldb0369 | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.705 |
| groEL | msrA | Ldb1617 | Ldb0673 | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.497 |
| groEL | polA | Ldb1617 | Ldb1512 | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.765 |
| groEL | trxA1 | Ldb1617 | Ldb1602 | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin; Belongs to the thioredoxin family. | 0.791 |
| groEL | trxA2 | Ldb1617 | Ldb1524 | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin. | 0.577 |
| groES | groEL | Ldb1618 | Ldb1617 | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| groES | hslO | Ldb1618 | Ldb0369 | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.629 |
| groES | msrA | Ldb1618 | Ldb0673 | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.504 |
| groES | polA | Ldb1618 | Ldb1512 | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.554 |
| groES | trxA1 | Ldb1618 | Ldb1602 | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Thioredoxin; Belongs to the thioredoxin family. | 0.623 |
| groES | trxA2 | Ldb1618 | Ldb1524 | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Thioredoxin. | 0.430 |
| hslO | groEL | Ldb0369 | Ldb1617 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.705 |
| hslO | groES | Ldb0369 | Ldb1618 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.629 |