| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| OAR04709.1 | htpX | SA87_09310 | SA87_06010 | Flagellar motor switch protein FliM; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.655 |
| OAR04897.1 | htpX | SA87_09855 | SA87_06010 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.590 |
| OAR05059.1 | htpX | SA87_06005 | SA87_06010 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.860 |
| dnaJ | dnaK | SA87_06040 | SA87_06035 | Molecular chaperone 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, [...] | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | ftsH | SA87_06040 | SA87_06395 | Molecular chaperone 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, [...] | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.834 |
| dnaJ | grpE | SA87_06040 | SA87_06030 | Molecular chaperone 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, [...] | Hypothetical 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-dep [...] | 0.997 |
| dnaJ | hrcA | SA87_06040 | SA87_06025 | Molecular chaperone 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, [...] | Hypothetical protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.918 |
| dnaJ | htpX | SA87_06040 | SA87_06010 | Molecular chaperone 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, [...] | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.724 |
| dnaJ | msrB | SA87_06040 | SA87_08085 | Molecular chaperone 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, [...] | 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. | 0.654 |
| dnaJ | secY | SA87_06040 | SA87_02160 | Molecular chaperone 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, [...] | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.640 |
| dnaK | dnaJ | SA87_06035 | SA87_06040 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone 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, [...] | 0.999 |
| dnaK | ftsH | SA87_06035 | SA87_06395 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.838 |
| dnaK | grpE | SA87_06035 | SA87_06030 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical 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-dep [...] | 0.999 |
| dnaK | hrcA | SA87_06035 | SA87_06025 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.968 |
| dnaK | htpX | SA87_06035 | SA87_06010 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.704 |
| dnaK | msrB | SA87_06035 | SA87_08085 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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. | 0.582 |
| dnaK | secY | SA87_06035 | SA87_02160 | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.856 |
| ftsH | dnaJ | SA87_06395 | SA87_06040 | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Molecular chaperone 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, [...] | 0.834 |
| ftsH | dnaK | SA87_06395 | SA87_06035 | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.838 |
| ftsH | grpE | SA87_06395 | SA87_06030 | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Hypothetical 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-dep [...] | 0.716 |