node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EFC05566.1 | dnaK | HMPREF9013_1269 | HMPREF9013_0216 | Phospholipase D domain protein; Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol; Belongs to the phospholipase D family. Cardiolipin synthase subfamily. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.653 |
EFC05566.1 | groS | HMPREF9013_1269 | HMPREF9013_0654 | Phospholipase D domain protein; Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol; Belongs to the phospholipase D family. Cardiolipin synthase subfamily. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.696 |
EFC06346.1 | dnaJ | HMPREF9013_1054 | HMPREF9013_0217 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | 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 [...] | 0.969 |
EFC06346.1 | dnaK | HMPREF9013_1054 | HMPREF9013_0216 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
EFC06346.1 | groL | HMPREF9013_1054 | HMPREF9013_0653 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.894 |
EFC06346.1 | groS | HMPREF9013_1054 | HMPREF9013_0654 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.752 |
EFC06346.1 | grpE | HMPREF9013_1054 | HMPREF9013_0215 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | Co-chaperone GrpE; 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-depend [...] | 0.760 |
EFC06346.1 | htpG | HMPREF9013_1054 | HMPREF9013_0702 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.995 |
EFC06346.1 | msrA | HMPREF9013_1054 | HMPREF9013_1398 | ATPase, AAA family; Identified by match to protein family HMM PF00004. | Peptide-methionine (S)-S-oxide 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. | 0.590 |
clpB | dnaJ | HMPREF9013_0218 | HMPREF9013_0217 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB 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 [...] | 0.971 |
clpB | dnaK | HMPREF9013_0218 | HMPREF9013_0216 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.987 |
clpB | groL | HMPREF9013_0218 | HMPREF9013_0653 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.700 |
clpB | groS | HMPREF9013_0218 | HMPREF9013_0654 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.712 |
clpB | grpE | HMPREF9013_0218 | HMPREF9013_0215 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | Co-chaperone GrpE; 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-depend [...] | 0.916 |
clpB | htpG | HMPREF9013_0218 | HMPREF9013_0702 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.726 |
clpB | msrA | HMPREF9013_0218 | HMPREF9013_1398 | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | Peptide-methionine (S)-S-oxide 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. | 0.544 |
dnaJ | EFC06346.1 | HMPREF9013_0217 | HMPREF9013_1054 | 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 [...] | ATPase, AAA family; Identified by match to protein family HMM PF00004. | 0.969 |
dnaJ | clpB | HMPREF9013_0217 | HMPREF9013_0218 | 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 [...] | Putative ATP-dependent chaperone protein ClpB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family. | 0.971 |
dnaJ | dnaK | HMPREF9013_0217 | HMPREF9013_0216 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groL | HMPREF9013_0217 | HMPREF9013_0653 | 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 GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.922 |