| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KMZ52468.1 | KMZ55887.1 | HMPREF0980_03484 | HMPREF0980_00004 | S4 RNA-binding domain protein. | Chaperone protein HtpG. | 0.595 |
| KMZ52468.1 | grpE | HMPREF0980_03484 | HMPREF0980_00588 | S4 RNA-binding domain protein. | Co-chaperone 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-depend [...] | 0.674 |
| KMZ52468.1 | hslO | HMPREF0980_03484 | HMPREF0980_00567 | S4 RNA-binding domain protein. | Chaperonin HslO; 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. | 0.872 |
| KMZ52468.1 | lon | HMPREF0980_03484 | HMPREF0980_00341 | S4 RNA-binding domain protein. | 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. | 0.467 |
| KMZ55218.1 | KMZ55221.1 | HMPREF0980_00566 | HMPREF0980_00569 | SAM dependent methyltransferase. | Putative redox family protein. | 0.606 |
| KMZ55218.1 | hslO | HMPREF0980_00566 | HMPREF0980_00567 | SAM dependent methyltransferase. | Chaperonin HslO; 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. | 0.842 |
| KMZ55218.1 | nadE | HMPREF0980_00566 | HMPREF0980_00568 | SAM dependent methyltransferase. | Glutamine-dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.688 |
| KMZ55221.1 | KMZ55218.1 | HMPREF0980_00569 | HMPREF0980_00566 | Putative redox family protein. | SAM dependent methyltransferase. | 0.606 |
| KMZ55221.1 | hslO | HMPREF0980_00569 | HMPREF0980_00567 | Putative redox family protein. | Chaperonin HslO; 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. | 0.676 |
| KMZ55221.1 | msrA | HMPREF0980_00569 | HMPREF0980_02749 | Putative redox family protein. | methionine-S-sulfoxide reductase/methionine-R-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. | 0.412 |
| KMZ55221.1 | nadE | HMPREF0980_00569 | HMPREF0980_00568 | Putative redox family protein. | Glutamine-dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.802 |
| KMZ55887.1 | KMZ52468.1 | HMPREF0980_00004 | HMPREF0980_03484 | Chaperone protein HtpG. | S4 RNA-binding domain protein. | 0.595 |
| KMZ55887.1 | groL | HMPREF0980_00004 | HMPREF0980_00471 | Chaperone protein HtpG. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.995 |
| KMZ55887.1 | grpE | HMPREF0980_00004 | HMPREF0980_00588 | Chaperone protein HtpG. | Co-chaperone 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-depend [...] | 0.893 |
| KMZ55887.1 | hslO | HMPREF0980_00004 | HMPREF0980_00567 | Chaperone protein HtpG. | Chaperonin HslO; 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. | 0.627 |
| KMZ55887.1 | lon | HMPREF0980_00004 | HMPREF0980_00341 | Chaperone protein HtpG. | 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. | 0.854 |
| KMZ55887.1 | msrA | HMPREF0980_00004 | HMPREF0980_02749 | Chaperone protein HtpG. | methionine-S-sulfoxide reductase/methionine-R-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. | 0.586 |
| coaX | hslO | HMPREF0980_01604 | HMPREF0980_00567 | Pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | Chaperonin HslO; 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. | 0.569 |
| groL | KMZ55887.1 | HMPREF0980_00471 | HMPREF0980_00004 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone protein HtpG. | 0.995 |
| groL | grpE | HMPREF0980_00471 | HMPREF0980_00588 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Co-chaperone 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-depend [...] | 0.989 |
