| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ldb0159 | Ldb0161 | Ldb0159 | Ldb0161 | Putative transcriptional regulator. | Conserved hypothetical protein; 5.2 Protein of unknown function similar to proteins from other organisms. | 0.464 |
| Ldb0159 | Ldb0162 | Ldb0159 | Ldb0162 | Putative transcriptional regulator. | Putative permease. | 0.458 |
| Ldb0159 | htpX1 | Ldb0159 | Ldb0160 | Putative transcriptional regulator. | Protease; Chaperone HtpX homologue; Belongs to the peptidase M48B family. | 0.492 |
| Ldb0161 | Ldb0159 | Ldb0161 | Ldb0159 | Conserved hypothetical protein; 5.2 Protein of unknown function similar to proteins from other organisms. | Putative transcriptional regulator. | 0.464 |
| Ldb0161 | Ldb0162 | Ldb0161 | Ldb0162 | Conserved hypothetical protein; 5.2 Protein of unknown function similar to proteins from other organisms. | Putative permease. | 0.497 |
| Ldb0161 | htpX1 | Ldb0161 | Ldb0160 | Conserved hypothetical protein; 5.2 Protein of unknown function similar to proteins from other organisms. | Protease; Chaperone HtpX homologue; Belongs to the peptidase M48B family. | 0.831 |
| Ldb0162 | Ldb0159 | Ldb0162 | Ldb0159 | Putative permease. | Putative transcriptional regulator. | 0.458 |
| Ldb0162 | Ldb0161 | Ldb0162 | Ldb0161 | Putative permease. | Conserved hypothetical protein; 5.2 Protein of unknown function similar to proteins from other organisms. | 0.497 |
| Ldb0162 | htpX1 | Ldb0162 | Ldb0160 | Putative permease. | Protease; Chaperone HtpX homologue; Belongs to the peptidase M48B family. | 0.467 |
| aspS | htpX1 | Ldb0889 | Ldb0160 | Aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Protease; Chaperone HtpX homologue; Belongs to the peptidase M48B family. | 0.490 |
| aspS | secY1 | Ldb0889 | Ldb0416 | Aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Preprotein translocase, SecY subunit; 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. | 0.431 |
| dnaJ | dnaK | Ldb1312 | Ldb1313 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Chaperone protein DnaK (heat shock protein); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | ftsH | Ldb1312 | Ldb0368 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | 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. | 0.741 |
| dnaJ | grpE | Ldb1312 | Ldb1314 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Chaperone protein GrpE (heat shock 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. Se [...] | 0.998 |
| dnaJ | hrcA | Ldb1312 | Ldb1315 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.945 |
| dnaJ | htpX1 | Ldb1312 | Ldb0160 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Protease; Chaperone HtpX homologue; Belongs to the peptidase M48B family. | 0.460 |
| dnaJ | secY1 | Ldb1312 | Ldb0416 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Preprotein translocase, SecY subunit; 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. | 0.424 |
| dnaK | dnaJ | Ldb1313 | Ldb1312 | Chaperone protein DnaK (heat shock protein); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | 0.999 |
| dnaK | ftsH | Ldb1313 | Ldb0368 | Chaperone protein DnaK (heat shock protein); 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 | Ldb1313 | Ldb1314 | Chaperone protein DnaK (heat shock protein); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein GrpE (heat shock 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. Se [...] | 0.999 |
