| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDS74568.1 | clpP | CLOSPI_01623 | CLOSPI_02165 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.504 |
| EDS74568.1 | dnaK | CLOSPI_01623 | CLOSPI_00865 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
| EDS74568.1 | dnaK-2 | CLOSPI_01623 | CLOSPI_01624 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.994 |
| EDS74568.1 | groL | CLOSPI_01623 | CLOSPI_00416 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.871 |
| EDS74568.1 | groS | CLOSPI_01623 | CLOSPI_00415 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.683 |
| EDS74568.1 | grpE | CLOSPI_01623 | CLOSPI_00866 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | 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 |
| EDS74568.1 | hrcA | CLOSPI_01623 | CLOSPI_00867 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | 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. | 0.548 |
| EDS74568.1 | htpG | CLOSPI_01623 | CLOSPI_00715 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.944 |
| EDS74568.1 | lon | CLOSPI_01623 | CLOSPI_00899 | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.652 |
| clpP | EDS74568.1 | CLOSPI_02165 | CLOSPI_01623 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | DnaJ domain protein; COG: COG2214 DnaJ-class molecular chaperone; Psort location: Cytoplasmic, score: 9.65. | 0.504 |
| clpP | dnaJ | CLOSPI_02165 | CLOSPI_00864 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.504 |
| clpP | dnaK | CLOSPI_02165 | CLOSPI_00865 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.431 |
| clpP | dnaK-2 | CLOSPI_02165 | CLOSPI_01624 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.431 |
| clpP | groL | CLOSPI_02165 | CLOSPI_00416 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.789 |
| clpP | groS | CLOSPI_02165 | CLOSPI_00415 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.821 |
| clpP | grpE | CLOSPI_02165 | CLOSPI_00866 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.733 |
| clpP | hrcA | CLOSPI_02165 | CLOSPI_00867 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 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. | 0.447 |
| clpP | htpG | CLOSPI_02165 | CLOSPI_00715 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.626 |
| clpP | lon | CLOSPI_02165 | CLOSPI_00899 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.751 |
| dnaJ | clpP | CLOSPI_00864 | CLOSPI_02165 | 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 [...] | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.504 |
