| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO46612.1 | ADO46613.1 | Entcl_0334 | Entcl_0335 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | KEGG: sei:SPC_3565 putative hydrolase; TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; PFAM: Haloacid dehalogenase domain protein hydrolase. | 0.951 |
| ADO46612.1 | ADO46614.1 | Entcl_0334 | Entcl_0336 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | PFAM: Intracellular growth attenuator IgaA; KEGG: kpn:KPN_03769 putative dehydrogenase. | 0.609 |
| ADO46612.1 | dnaJ | Entcl_0334 | Entcl_3704 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | 0.642 |
| ADO46612.1 | grpE | Entcl_0334 | Entcl_1109 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 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 [...] | 0.636 |
| ADO46612.1 | hslO | Entcl_0334 | Entcl_0333 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | Hsp33 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. | 0.973 |
| ADO46612.1 | hslU | Entcl_0334 | Entcl_4343 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.715 |
| ADO46612.1 | hslV | Entcl_0334 | Entcl_4342 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.735 |
| ADO46612.1 | htpG | Entcl_0334 | Entcl_3317 | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | Heat shock protein Hsp90-like protein; Molecular chaperone. Has ATPase activity. | 0.549 |
| ADO46613.1 | ADO46612.1 | Entcl_0335 | Entcl_0334 | KEGG: sei:SPC_3565 putative hydrolase; TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; PFAM: Haloacid dehalogenase domain protein hydrolase. | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | 0.951 |
| ADO46613.1 | ADO46614.1 | Entcl_0335 | Entcl_0336 | KEGG: sei:SPC_3565 putative hydrolase; TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; PFAM: Haloacid dehalogenase domain protein hydrolase. | PFAM: Intracellular growth attenuator IgaA; KEGG: kpn:KPN_03769 putative dehydrogenase. | 0.623 |
| ADO46613.1 | hslO | Entcl_0335 | Entcl_0333 | KEGG: sei:SPC_3565 putative hydrolase; TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; PFAM: Haloacid dehalogenase domain protein hydrolase. | Hsp33 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. | 0.808 |
| ADO46614.1 | ADO46612.1 | Entcl_0336 | Entcl_0334 | PFAM: Intracellular growth attenuator IgaA; KEGG: kpn:KPN_03769 putative dehydrogenase. | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | 0.609 |
| ADO46614.1 | ADO46613.1 | Entcl_0336 | Entcl_0335 | PFAM: Intracellular growth attenuator IgaA; KEGG: kpn:KPN_03769 putative dehydrogenase. | KEGG: sei:SPC_3565 putative hydrolase; TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; PFAM: Haloacid dehalogenase domain protein hydrolase. | 0.623 |
| ADO46614.1 | hslO | Entcl_0336 | Entcl_0333 | PFAM: Intracellular growth attenuator IgaA; KEGG: kpn:KPN_03769 putative dehydrogenase. | Hsp33 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. | 0.626 |
| dnaJ | ADO46612.1 | Entcl_3704 | Entcl_0334 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | RNA-binding S4 domain protein; KEGG: sdy:SDY_3678 ribosome-associated heat shock protein HSP15; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; Belongs to the HSP15 family. | 0.642 |
| dnaJ | groL | Entcl_3704 | Entcl_4010 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.977 |
| dnaJ | grpE | Entcl_3704 | Entcl_1109 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | 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 |
| dnaJ | hslO | Entcl_3704 | Entcl_0333 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | Hsp33 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. | 0.705 |
| dnaJ | hslU | Entcl_3704 | Entcl_4343 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.969 |
| dnaJ | hslV | Entcl_3704 | Entcl_4342 | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...] | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.955 |