| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpL | clpP | SSA_2096 | SSA_1731 | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | 0.961 |
| clpL | dnaJ | SSA_2096 | SSA_2005 | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | Chaperone protein dnaJ, putative; 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 betwe [...] | 0.789 |
| clpL | dnaK | SSA_2096 | SSA_2007 | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | Chaperone protein dnaK/HSP70, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.908 |
| clpL | groEL | SSA_2096 | SSA_0226 | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.843 |
| clpL | groS | SSA_2096 | SSA_0225 | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.705 |
| clpL | grpE | SSA_2096 | SSA_2008 | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE (HSP-70 cofactor), putative; 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 [...] | 0.722 |
| clpP | clpL | SSA_1731 | SSA_2096 | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | 0.961 |
| clpP | dnaJ | SSA_1731 | SSA_2005 | ATP-dependent Clp protease, proteolytic subunit, putative; 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, putative; 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 betwe [...] | 0.658 |
| clpP | dnaK | SSA_1731 | SSA_2007 | ATP-dependent Clp protease, proteolytic subunit, putative; 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/HSP70, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.723 |
| clpP | groEL | SSA_1731 | SSA_0226 | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.850 |
| clpP | groS | SSA_1731 | SSA_0225 | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.833 |
| clpP | grpE | SSA_1731 | SSA_2008 | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | Molecular chaperone GrpE (HSP-70 cofactor), putative; 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 [...] | 0.736 |
| clpP | hrcA | SSA_1731 | SSA_2009 | ATP-dependent Clp protease, proteolytic subunit, putative; 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 shock transcription repressor HrcA, putative; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.578 |
| clpP | hslO | SSA_1731 | SSA_2190 | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | 33 kDa chaperonin, putative; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.401 |
| clpP | polA | SSA_1731 | SSA_0100 | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | DNA polymerase I - 3'-5' exonuclease and polymerase domains, putative; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.762 |
| dnaJ | clpL | SSA_2005 | SSA_2096 | Chaperone protein dnaJ, putative; 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 betwe [...] | ATP-dependent protease, ATP-binding subunit, putative; GC: 47.36%; Codon Adaptation Index (CAI): 0.799; Protein involved in nucleoside-triphosphatase activity; Belongs to the ClpA/ClpB family. | 0.789 |
| dnaJ | clpP | SSA_2005 | SSA_1731 | Chaperone protein dnaJ, putative; 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 betwe [...] | ATP-dependent Clp protease, proteolytic subunit, putative; 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. | 0.658 |
| dnaJ | dnaK | SSA_2005 | SSA_2007 | Chaperone protein dnaJ, putative; 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 betwe [...] | Chaperone protein dnaK/HSP70, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL | SSA_2005 | SSA_0226 | Chaperone protein dnaJ, putative; 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 betwe [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.948 |
| dnaJ | groS | SSA_2005 | SSA_0225 | Chaperone protein dnaJ, putative; 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 betwe [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.887 |
