| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| b0053 | cbpA | CH53_1056 | CH53_2649 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | Putative chaperone DnaJ. | 0.541 |
| b0053 | dnaJ | CH53_1056 | CH53_1076 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | 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 [...] | 0.541 |
| b0053 | dnaK | CH53_1056 | CH53_1077 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.558 |
| b0053 | hdeB | CH53_1056 | CH53_722 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | hdeB domain protein; Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. Belongs to the HdeB family. | 0.530 |
| b0053 | hscB | CH53_1056 | CH53_643 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | Fe-S protein assembly co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.557 |
| b0053 | htpG | CH53_1056 | CH53_2903 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | Hsp90 family protein; Molecular chaperone. Has ATPase activity. | 0.548 |
| b0053 | uspA | CH53_1056 | CH53_1607 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | Universal stress protein A. | 0.618 |
| b0053 | uspE | CH53_1056 | CH53_4024 | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | Universal stress protein E. | 0.664 |
| cbpA | b0053 | CH53_2649 | CH53_1056 | Putative chaperone DnaJ. | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | 0.541 |
| cbpA | dnaK | CH53_2649 | CH53_1077 | Putative chaperone DnaJ. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.981 |
| cbpA | hdeB | CH53_2649 | CH53_722 | Putative chaperone DnaJ. | hdeB domain protein; Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. Belongs to the HdeB family. | 0.554 |
| cbpA | hscB | CH53_2649 | CH53_643 | Putative chaperone DnaJ. | Fe-S protein assembly co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.569 |
| cbpA | htpG | CH53_2649 | CH53_2903 | Putative chaperone DnaJ. | Hsp90 family protein; Molecular chaperone. Has ATPase activity. | 0.889 |
| cbpA | uspA | CH53_2649 | CH53_1607 | Putative chaperone DnaJ. | Universal stress protein A. | 0.571 |
| cbpA | uspE | CH53_2649 | CH53_4024 | Putative chaperone DnaJ. | Universal stress protein E. | 0.617 |
| dnaJ | b0053 | CH53_1076 | CH53_1056 | 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 [...] | PPIC-type PPIASE domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | 0.541 |
| dnaJ | dnaK | CH53_1076 | CH53_1077 | 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 | hdeB | CH53_1076 | CH53_722 | 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 [...] | hdeB domain protein; Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. Belongs to the HdeB family. | 0.542 |
| dnaJ | hscB | CH53_1076 | CH53_643 | 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 [...] | Fe-S protein assembly co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.554 |
| dnaJ | htpG | CH53_1076 | CH53_2903 | 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 [...] | Hsp90 family protein; Molecular chaperone. Has ATPase activity. | 0.980 |
