node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SMB86431.1 | SMB93303.1 | SAMN00017405_1160 | SAMN00017405_0016 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein. | InterPro IPR008616:IPR008532:IPR006025; COGs: COG1293 RNA-binding protein homologous to eukaryotic snRNP; KEGG: pca:Pcar_1454 RNA-binding protein; SPTR: A2UB94 Fibronectin-binding A-like; PFAM: Fibronectin-binding A domain protein; protein of unknown function DUF814. | 0.874 |
SMB86431.1 | grpE | SAMN00017405_1160 | SAMN00017405_1378 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein. | 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 [...] | 0.568 |
SMB86431.1 | hslO | SAMN00017405_1160 | SAMN00017405_0039 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein. | Molecular chaperone Hsp33; 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. | 0.847 |
SMB86431.1 | hslU | SAMN00017405_1160 | SAMN00017405_0125 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein. | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.591 |
SMB86431.1 | hslV | SAMN00017405_1160 | SAMN00017405_0124 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein. | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.669 |
SMB90879.1 | dnaJ | SAMN00017405_1377 | SAMN00017405_1380 | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | 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, [...] | 0.906 |
SMB90879.1 | grpE | SAMN00017405_1377 | SAMN00017405_1378 | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | 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 [...] | 0.986 |
SMB90879.1 | hslO | SAMN00017405_1377 | SAMN00017405_0039 | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | Molecular chaperone Hsp33; 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. | 0.563 |
SMB90879.1 | hslU | SAMN00017405_1377 | SAMN00017405_0125 | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.721 |
SMB90879.1 | hslV | SAMN00017405_1377 | SAMN00017405_0124 | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.695 |
SMB90879.1 | msrA | SAMN00017405_1377 | SAMN00017405_0783 | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | Peptide methionine sulfoxide reductase msrA/msrB; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.581 |
SMB93303.1 | SMB86431.1 | SAMN00017405_0016 | SAMN00017405_1160 | InterPro IPR008616:IPR008532:IPR006025; COGs: COG1293 RNA-binding protein homologous to eukaryotic snRNP; KEGG: pca:Pcar_1454 RNA-binding protein; SPTR: A2UB94 Fibronectin-binding A-like; PFAM: Fibronectin-binding A domain protein; protein of unknown function DUF814. | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein. | 0.874 |
SMB93303.1 | hslO | SAMN00017405_0016 | SAMN00017405_0039 | InterPro IPR008616:IPR008532:IPR006025; COGs: COG1293 RNA-binding protein homologous to eukaryotic snRNP; KEGG: pca:Pcar_1454 RNA-binding protein; SPTR: A2UB94 Fibronectin-binding A-like; PFAM: Fibronectin-binding A domain protein; protein of unknown function DUF814. | Molecular chaperone Hsp33; 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. | 0.531 |
SMB93455.1 | hslO | SAMN00017405_0038 | SAMN00017405_0039 | Riboflavin transporter FmnP; Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins; Belongs to the prokaryotic riboflavin transporter (P-RFT) (TC 2.A.87) family. | Molecular chaperone Hsp33; 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. | 0.576 |
dnaJ | SMB90879.1 | SAMN00017405_1380 | SAMN00017405_1377 | 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, [...] | Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1. | 0.906 |
dnaJ | groL | SAMN00017405_1380 | SAMN00017405_2394 | 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, [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.859 |
dnaJ | grpE | SAMN00017405_1380 | SAMN00017405_1378 | 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 [...] | 0.992 |
dnaJ | hslO | SAMN00017405_1380 | SAMN00017405_0039 | 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 Hsp33; 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. | 0.638 |
dnaJ | hslU | SAMN00017405_1380 | SAMN00017405_0125 | 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, [...] | ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.687 |
dnaJ | hslV | SAMN00017405_1380 | SAMN00017405_0124 | 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, [...] | ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.563 |