node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CUM76376.1 | hslO | ERS852572_00363 | ERS852572_02645 | Photosystem II S4 domain protein. | Heat shock protein 33 homolog; 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. | 0.541 |
CUM76376.1 | mrnC | ERS852572_00363 | ERS852572_00401 | Photosystem II S4 domain protein. | Mini-ribonuclease 3; Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors; Belongs to the MrnC RNase family. | 0.741 |
CUN12688.1 | grpE | ERS852572_02037 | ERS852572_00075 | S4 domain. | HSP-70 cofactor; 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-dependen [...] | 0.584 |
CUN12688.1 | hslO | ERS852572_02037 | ERS852572_02645 | S4 domain. | Heat shock protein 33 homolog; 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. | 0.816 |
CUN22680.1 | hslO | ERS852572_02643 | ERS852572_02645 | Uncharacterized oxidoreductase Mb2996. | Heat shock protein 33 homolog; 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. | 0.518 |
CUN22680.1 | nadE | ERS852572_02643 | ERS852572_02644 | Uncharacterized oxidoreductase Mb2996. | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.778 |
bsmA | hslO | ERS852572_02646 | ERS852572_02645 | Glycine/sarcosine N-methyltransferase. | Heat shock protein 33 homolog; 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. | 0.767 |
bsmA | nadE | ERS852572_02646 | ERS852572_02644 | Glycine/sarcosine N-methyltransferase. | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.522 |
groL | grpE | ERS852572_02348 | ERS852572_00075 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | HSP-70 cofactor; 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-dependen [...] | 0.994 |
groL | hslO | ERS852572_02348 | ERS852572_02645 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein 33 homolog; 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. | 0.641 |
groL | lon1 | ERS852572_02348 | ERS852572_01458 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Lon protease 1; 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. | 0.823 |
groL | nadE | ERS852572_02348 | ERS852572_02644 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.641 |
grpE | CUN12688.1 | ERS852572_00075 | ERS852572_02037 | HSP-70 cofactor; 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-dependen [...] | S4 domain. | 0.584 |
grpE | groL | ERS852572_00075 | ERS852572_02348 | HSP-70 cofactor; 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-dependen [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.994 |
grpE | hslO | ERS852572_00075 | ERS852572_02645 | HSP-70 cofactor; 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-dependen [...] | Heat shock protein 33 homolog; 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. | 0.660 |
grpE | lon1 | ERS852572_00075 | ERS852572_01458 | HSP-70 cofactor; 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-dependen [...] | Lon protease 1; 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 |
grpE | ribD_2 | ERS852572_00075 | ERS852572_03396 | HSP-70 cofactor; 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-dependen [...] | Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. | 0.706 |
hslO | CUM76376.1 | ERS852572_02645 | ERS852572_00363 | Heat shock protein 33 homolog; 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. | Photosystem II S4 domain protein. | 0.541 |
hslO | CUN12688.1 | ERS852572_02645 | ERS852572_02037 | Heat shock protein 33 homolog; 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. | S4 domain. | 0.816 |
hslO | CUN22680.1 | ERS852572_02645 | ERS852572_02643 | Heat shock protein 33 homolog; 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. | Uncharacterized oxidoreductase Mb2996. | 0.518 |