| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| NMB1138 | hslO | NMB1138 | NMB2000 | Conserved hypothetical protein; Identified by similarity to EGAD:29941; match to protein family HMM PF01479. | Conserved hypothetical protein; 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. | 0.683 |
| NMB1176 | hslO | NMB1176 | NMB2000 | Conserved hypothetical protein; Identified by similarity to EGAD:29941; match to protein family HMM PF01479. | Conserved hypothetical protein; 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. | 0.682 |
| NMB2001 | NMB2002 | NMB2001 | NMB2002 | Conserved hypothetical protein; Identified by similarity to EGAD:91561; match to protein family HMM PF00877. | Hypothetical protein; Identified by Glimmer2; putative. | 0.774 |
| NMB2001 | hslO | NMB2001 | NMB2000 | Conserved hypothetical protein; Identified by similarity to EGAD:91561; match to protein family HMM PF00877. | Conserved hypothetical protein; 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. | 0.458 |
| NMB2002 | NMB2001 | NMB2002 | NMB2001 | Hypothetical protein; Identified by Glimmer2; putative. | Conserved hypothetical protein; Identified by similarity to EGAD:91561; match to protein family HMM PF00877. | 0.774 |
| NMB2002 | hslO | NMB2002 | NMB2000 | Hypothetical protein; Identified by Glimmer2; putative. | Conserved hypothetical protein; 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. | 0.464 |
| NMB2002 | pilB | NMB2002 | NMB0044 | Hypothetical protein; Identified by Glimmer2; putative. | 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 (By similarity). | 0.572 |
| dnaK | groEL | NMB0554 | NMB1972 | dnaK protein; Acts as a chaperone. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.978 |
| dnaK | groES | NMB0554 | NMB1973 | dnaK protein; Acts as a chaperone. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.956 |
| dnaK | grpE | NMB0554 | NMB0561 | dnaK protein; Acts as a chaperone. | grpE protein; 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-dependent i [...] | 0.990 |
| dnaK | hslO | NMB0554 | NMB2000 | dnaK protein; Acts as a chaperone. | Conserved hypothetical protein; 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. | 0.460 |
| dnaK | lon | NMB0554 | NMB1231 | dnaK protein; Acts as a chaperone. | ATP-dependent protease La; 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. | 0.541 |
| dnaK | pilB | NMB0554 | NMB0044 | dnaK protein; Acts as a chaperone. | 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 (By similarity). | 0.694 |
| groEL | dnaK | NMB1972 | NMB0554 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | dnaK protein; Acts as a chaperone. | 0.978 |
| groEL | groES | NMB1972 | NMB1973 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
| groEL | grpE | NMB1972 | NMB0561 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | grpE protein; 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-dependent i [...] | 0.984 |
| groEL | hslO | NMB1972 | NMB2000 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Conserved hypothetical protein; 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. | 0.695 |
| groEL | lon | NMB1972 | NMB1231 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | ATP-dependent protease La; 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. | 0.818 |
| groEL | pilB | NMB1972 | NMB0044 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) 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 (By similarity). | 0.774 |
| groES | dnaK | NMB1973 | NMB0554 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | dnaK protein; Acts as a chaperone. | 0.956 |