| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALZ85709.1 | cyaY | APT59_16425 | APT59_20795 | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 0.982 |
| ALZ85709.1 | hscA | APT59_16425 | APT59_16410 | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 2Fe-2S ferredoxin; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.982 |
| ALZ85709.1 | hscB | APT59_16425 | APT59_16415 | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 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. | 0.998 |
| ALZ85709.1 | iscA | APT59_16425 | APT59_16420 | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Iron-sulfur cluster assembly protein IscA; Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system; Belongs to the HesB/IscA family. | 0.986 |
| ALZ85709.1 | iscS | APT59_16425 | APT59_16430 | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | 0.999 |
| ALZ85709.1 | iscX | APT59_16425 | APT59_16400 | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Fe-S assembly protein IscX; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.914 |
| ALZ85917.1 | grpE | APT59_17555 | APT59_02250 | DNA-binding protein; Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.903 |
| ALZ85917.1 | hscA | APT59_17555 | APT59_16410 | DNA-binding protein; Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2Fe-2S ferredoxin; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.877 |
| ALZ85917.1 | htpG | APT59_17555 | APT59_07015 | DNA-binding protein; Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.849 |
| cyaY | ALZ85709.1 | APT59_20795 | APT59_16425 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Scaffolding protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 0.982 |
| cyaY | hscA | APT59_20795 | APT59_16410 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 2Fe-2S ferredoxin; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.895 |
| cyaY | hscB | APT59_20795 | APT59_16415 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | 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. | 0.916 |
| cyaY | iscA | APT59_20795 | APT59_16420 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Iron-sulfur cluster assembly protein IscA; Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system; Belongs to the HesB/IscA family. | 0.567 |
| cyaY | iscS | APT59_20795 | APT59_16430 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | 0.909 |
| cyaY | iscX | APT59_20795 | APT59_16400 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Fe-S assembly protein IscX; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.808 |
| dnaJ | grpE | APT59_02260 | APT59_02250 | Molecular chaperone 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, [...] | Molecular 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 [...] | 0.982 |
| dnaJ | hscA | APT59_02260 | APT59_16410 | Molecular chaperone 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, [...] | 2Fe-2S ferredoxin; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.963 |
| dnaJ | htpG | APT59_02260 | APT59_07015 | Molecular chaperone 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, [...] | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.970 |
| grpE | ALZ85917.1 | APT59_02250 | APT59_17555 | Molecular 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 [...] | DNA-binding protein; Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.903 |
| grpE | dnaJ | APT59_02250 | APT59_02260 | Molecular 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 [...] | Molecular chaperone 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, [...] | 0.982 |