node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BPSS1143 | groEL | BPSS1143 | BPSL2697 | Putative formate hydrogenlyase/hydrogenase/NADH dehydrogenase subunit; Similar to Escherichia coli formate hydrogenlyase subunit 5 precursor HycE or HevE or b2721 SWALL:HYCE_ECOLI (SWALL:P16431) (569 aa) fasta scores: E(): 2.5e-31, 31.25% id in 464 aa, and to Methanosarcina acetivorans hydrogenase-3, subunit E ma4372 SWALL:Q8THY6 (EMBL:AE011156) (545 aa) fasta scores: E(): 9.1e-42, 38.47% id in 473 aa, and to Mycobacterium tuberculosis probable formate hydrogenlyase cy251.05 rv0087 or mtcy251.05 SWALL:Q10884 (EMBL:Z74410) (492 aa) fasta scores: E(): 1.4e-39, 42.22% id in 450 aa. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.936 |
BPSS1143 | groL | BPSS1143 | BPSS0477 | Putative formate hydrogenlyase/hydrogenase/NADH dehydrogenase subunit; Similar to Escherichia coli formate hydrogenlyase subunit 5 precursor HycE or HevE or b2721 SWALL:HYCE_ECOLI (SWALL:P16431) (569 aa) fasta scores: E(): 2.5e-31, 31.25% id in 464 aa, and to Methanosarcina acetivorans hydrogenase-3, subunit E ma4372 SWALL:Q8THY6 (EMBL:AE011156) (545 aa) fasta scores: E(): 9.1e-42, 38.47% id in 473 aa, and to Mycobacterium tuberculosis probable formate hydrogenlyase cy251.05 rv0087 or mtcy251.05 SWALL:Q10884 (EMBL:Z74410) (492 aa) fasta scores: E(): 1.4e-39, 42.22% id in 450 aa. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.936 |
dnaJ | dnaK | BPSL2826 | BPSL2827 | Putative DnaJ chaperone 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 interactions betwee [...] | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
dnaJ | groEL | BPSL2826 | BPSL2697 | Putative DnaJ chaperone 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 interactions betwee [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.892 |
dnaJ | groES1 | BPSL2826 | BPSL2698 | Putative DnaJ chaperone 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 interactions betwee [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.826 |
dnaJ | groES2 | BPSL2826 | BPSL2919 | Putative DnaJ chaperone 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 interactions betwee [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.828 |
dnaJ | groL | BPSL2826 | BPSS0477 | Putative DnaJ chaperone 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 interactions betwee [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.899 |
dnaJ | groS | BPSL2826 | BPSS0476 | Putative DnaJ chaperone 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 interactions betwee [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.828 |
dnaJ | grpE | BPSL2826 | BPSL2829 | Putative DnaJ chaperone 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 interactions betwee [...] | Conserved hypothetical protein (pseudogene); 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 [...] | 0.997 |
dnaJ | htpG | BPSL2826 | BPSL1087 | Putative DnaJ chaperone 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 interactions betwee [...] | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.996 |
dnaJ | rpoH | BPSL2826 | BPSL0504 | Putative DnaJ chaperone 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 interactions betwee [...] | RNA polymerase sigma-32 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.904 |
dnaK | dnaJ | BPSL2827 | BPSL2826 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative DnaJ chaperone 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 interactions betwee [...] | 0.998 |
dnaK | groEL | BPSL2827 | BPSL2697 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.934 |
dnaK | groES1 | BPSL2827 | BPSL2698 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.832 |
dnaK | groES2 | BPSL2827 | BPSL2919 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.834 |
dnaK | groL | BPSL2827 | BPSS0477 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.935 |
dnaK | groS | BPSL2827 | BPSS0476 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.834 |
dnaK | grpE | BPSL2827 | BPSL2829 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Conserved hypothetical protein (pseudogene); 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 [...] | 0.988 |
dnaK | htpG | BPSL2827 | BPSL1087 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.973 |
dnaK | rpoH | BPSL2827 | BPSL0504 | Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | RNA polymerase sigma-32 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.712 |