| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB86440.1 | htpX | Alide2_4122 | Alide2_4123 | KEGG: dia:Dtpsy_3022 hypothetical protein. | PFAM: Peptidase M48; KEGG: ajs:Ajs_3742 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.590 |
| AEB86442.1 | htpX | Alide2_4124 | Alide2_4123 | KEGG: ajs:Ajs_3743 putative transmembrane protein. | PFAM: Peptidase M48; KEGG: ajs:Ajs_3742 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.565 |
| AEB86442.1 | pyrC | Alide2_4124 | Alide2_4125 | KEGG: ajs:Ajs_3743 putative transmembrane protein. | Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | 0.842 |
| AEB86783.1 | dnaJ | Alide2_4480 | Alide2_1320 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 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 [...] | 0.807 |
| AEB86783.1 | ftsH | Alide2_4480 | Alide2_2059 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | ATP-dependent metalloprotease 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. | 0.771 |
| AEB86783.1 | ftsH-2 | Alide2_4480 | Alide2_2675 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | ATP-dependent metalloprotease 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. | 0.771 |
| AEB86783.1 | ftsH-3 | Alide2_4480 | Alide2_4290 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | ATP-dependent metalloprotease 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. | 0.771 |
| AEB86783.1 | grpE | Alide2_4480 | Alide2_1322 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 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 [...] | 0.870 |
| AEB86783.1 | htpX | Alide2_4480 | Alide2_4123 | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | PFAM: Peptidase M48; KEGG: ajs:Ajs_3742 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.564 |
| dnaJ | AEB86783.1 | Alide2_1320 | Alide2_4480 | 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 [...] | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 0.807 |
| dnaJ | ftsH | Alide2_1320 | Alide2_2059 | 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 [...] | ATP-dependent metalloprotease 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. | 0.585 |
| dnaJ | ftsH-2 | Alide2_1320 | Alide2_2675 | 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 [...] | ATP-dependent metalloprotease 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. | 0.698 |
| dnaJ | ftsH-3 | Alide2_1320 | Alide2_4290 | 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 [...] | ATP-dependent metalloprotease 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. | 0.630 |
| dnaJ | grpE | Alide2_1320 | Alide2_1322 | 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 | htpX | Alide2_1320 | Alide2_4123 | 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 [...] | PFAM: Peptidase M48; KEGG: ajs:Ajs_3742 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.485 |
| dnaJ | secY | Alide2_1320 | Alide2_4357 | 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 [...] | 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. | 0.415 |
| ftsH | AEB86783.1 | Alide2_2059 | Alide2_4480 | ATP-dependent metalloprotease 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. | Thioredoxin; KEGG: dia:Dtpsy_3279 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain. | 0.771 |
| ftsH | dnaJ | Alide2_2059 | Alide2_1320 | ATP-dependent metalloprotease 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. | 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 [...] | 0.585 |
| ftsH | grpE | Alide2_2059 | Alide2_1322 | ATP-dependent metalloprotease 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. | 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 [...] | 0.545 |
| ftsH | htpX | Alide2_2059 | Alide2_4123 | ATP-dependent metalloprotease 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. | PFAM: Peptidase M48; KEGG: ajs:Ajs_3742 heat shock protein HtpX; Belongs to the peptidase M48B family. | 0.627 |
