| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KXA30502.1 | KXA31478.1 | HMPREF3229_00965 | HMPREF3229_00466 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | 0.862 |
| KXA30502.1 | dnaJ_2 | HMPREF3229_00965 | HMPREF3229_01263 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase 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 [...] | 0.806 |
| KXA30502.1 | dnaK | HMPREF3229_00965 | HMPREF3229_01264 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.944 |
| KXA30502.1 | htpG | HMPREF3229_00965 | HMPREF3229_00539 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.959 |
| KXA30502.1 | resA_2 | HMPREF3229_00965 | HMPREF3229_01353 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Redoxin family protein; KEGG: aca:ACP_1678 1.6e-11 thiol-disulfide oxidoreductase. | 0.842 |
| KXA31478.1 | KXA30502.1 | HMPREF3229_00466 | HMPREF3229_00965 | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.862 |
| KXA31478.1 | dnaJ_2 | HMPREF3229_00466 | HMPREF3229_01263 | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | 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 [...] | 0.910 |
| KXA31478.1 | dnaK | HMPREF3229_00466 | HMPREF3229_01264 | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.955 |
| KXA31478.1 | groL | HMPREF3229_00466 | HMPREF3229_01781 | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.471 |
| KXA31478.1 | htpG | HMPREF3229_00466 | HMPREF3229_00539 | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.959 |
| KXA31478.1 | resA_2 | HMPREF3229_00466 | HMPREF3229_01353 | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | Redoxin family protein; KEGG: aca:ACP_1678 1.6e-11 thiol-disulfide oxidoreductase. | 0.789 |
| dnaJ_2 | KXA30502.1 | HMPREF3229_01263 | HMPREF3229_00965 | 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 [...] | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.806 |
| dnaJ_2 | KXA31478.1 | HMPREF3229_01263 | HMPREF3229_00466 | 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 [...] | Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50. | 0.910 |
| dnaJ_2 | dnaK | HMPREF3229_01263 | HMPREF3229_01264 | 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. | 0.997 |
| dnaJ_2 | groL | HMPREF3229_01263 | HMPREF3229_01781 | 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. | 0.816 |
| dnaJ_2 | grpE | HMPREF3229_01263 | HMPREF3229_01265 | 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 [...] | 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 [...] | 0.969 |
| dnaJ_2 | htpG | HMPREF3229_01263 | HMPREF3229_00539 | 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 HtpG; Molecular chaperone. Has ATPase activity. | 0.945 |
| dnaJ_2 | miaB_1 | HMPREF3229_01263 | HMPREF3229_01260 | 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 [...] | tRNA methylthiotransferase YqeV; KEGG: cdf:CD2448 8.8e-114 radical SAM superfamily protein; K08070 2-alkenal reductase; Psort location: Cytoplasmic, score: 7.50. | 0.779 |
| dnaJ_2 | prmA | HMPREF3229_01263 | HMPREF3229_01262 | 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 [...] | Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. | 0.882 |
| dnaJ_2 | resA_2 | HMPREF3229_01263 | HMPREF3229_01353 | 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 [...] | Redoxin family protein; KEGG: aca:ACP_1678 1.6e-11 thiol-disulfide oxidoreductase. | 0.787 |
