| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB84481.1 | AEB86127.1 | Alide2_2109 | Alide2_3802 | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | Hsp33 protein; 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; Belongs to the HSP33 family. | 0.832 |
| AEB84481.1 | dnaJ | Alide2_2109 | Alide2_1320 | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | 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 [...] | 0.637 |
| AEB84481.1 | grpE | Alide2_2109 | Alide2_1322 | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | GrpE protein; 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-dependent i [...] | 0.618 |
| AEB84481.1 | hslU | Alide2_2109 | Alide2_4069 | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | Heat shock protein HslVU, ATPase 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. | 0.650 |
| AEB84481.1 | hslV | Alide2_2109 | Alide2_4070 | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.775 |
| AEB84481.1 | htpG | Alide2_2109 | Alide2_0508 | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.464 |
| AEB86126.1 | AEB86127.1 | Alide2_3801 | Alide2_3802 | ABC-type transporter, periplasmic subunit family 3; KEGG: xtr:100498246 histidine-binding periplasmic protein-like; PFAM: Extracellular solute-binding protein, family 3; SMART: Extracellular solute-binding protein, family 3; Belongs to the bacterial solute-binding protein 3 family. | Hsp33 protein; 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; Belongs to the HSP33 family. | 0.586 |
| AEB86126.1 | AEB86128.1 | Alide2_3801 | Alide2_3803 | ABC-type transporter, periplasmic subunit family 3; KEGG: xtr:100498246 histidine-binding periplasmic protein-like; PFAM: Extracellular solute-binding protein, family 3; SMART: Extracellular solute-binding protein, family 3; Belongs to the bacterial solute-binding protein 3 family. | KEGG: ajs:Ajs_0993 transferase hexapeptide protein. | 0.585 |
| AEB86126.1 | AEB86129.1 | Alide2_3801 | Alide2_3804 | ABC-type transporter, periplasmic subunit family 3; KEGG: xtr:100498246 histidine-binding periplasmic protein-like; PFAM: Extracellular solute-binding protein, family 3; SMART: Extracellular solute-binding protein, family 3; Belongs to the bacterial solute-binding protein 3 family. | KEGG: dia:Dtpsy_0907 protein of unknown function DUF455; manually curated; PFAM: Protein of unknown function DUF455. | 0.453 |
| AEB86127.1 | AEB84481.1 | Alide2_3802 | Alide2_2109 | Hsp33 protein; 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; Belongs to the HSP33 family. | KEGG: ajs:Ajs_1639 RNA-binding S4 domain-containing protein; PFAM: RNA-binding S4; SMART: RNA-binding S4. | 0.832 |
| AEB86127.1 | AEB86126.1 | Alide2_3802 | Alide2_3801 | Hsp33 protein; 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; Belongs to the HSP33 family. | ABC-type transporter, periplasmic subunit family 3; KEGG: xtr:100498246 histidine-binding periplasmic protein-like; PFAM: Extracellular solute-binding protein, family 3; SMART: Extracellular solute-binding protein, family 3; Belongs to the bacterial solute-binding protein 3 family. | 0.586 |
| AEB86127.1 | AEB86128.1 | Alide2_3802 | Alide2_3803 | Hsp33 protein; 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; Belongs to the HSP33 family. | KEGG: ajs:Ajs_0993 transferase hexapeptide protein. | 0.837 |
| AEB86127.1 | AEB86129.1 | Alide2_3802 | Alide2_3804 | Hsp33 protein; 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; Belongs to the HSP33 family. | KEGG: dia:Dtpsy_0907 protein of unknown function DUF455; manually curated; PFAM: Protein of unknown function DUF455. | 0.700 |
| AEB86127.1 | dnaJ | Alide2_3802 | Alide2_1320 | Hsp33 protein; 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; Belongs to the HSP33 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 [...] | 0.608 |
| AEB86127.1 | grpE | Alide2_3802 | Alide2_1322 | Hsp33 protein; 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; Belongs to the HSP33 family. | GrpE protein; 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-dependent i [...] | 0.605 |
| AEB86127.1 | hslU | Alide2_3802 | Alide2_4069 | Hsp33 protein; 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; Belongs to the HSP33 family. | Heat shock protein HslVU, ATPase 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. | 0.781 |
| AEB86127.1 | hslV | Alide2_3802 | Alide2_4070 | Hsp33 protein; 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; Belongs to the HSP33 family. | ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.720 |
| AEB86127.1 | htpG | Alide2_3802 | Alide2_0508 | Hsp33 protein; 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; Belongs to the HSP33 family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.562 |
| AEB86127.1 | tig | Alide2_3802 | Alide2_1458 | Hsp33 protein; 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; Belongs to the HSP33 family. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.649 |
| AEB86128.1 | AEB86126.1 | Alide2_3803 | Alide2_3801 | KEGG: ajs:Ajs_0993 transferase hexapeptide protein. | ABC-type transporter, periplasmic subunit family 3; KEGG: xtr:100498246 histidine-binding periplasmic protein-like; PFAM: Extracellular solute-binding protein, family 3; SMART: Extracellular solute-binding protein, family 3; Belongs to the bacterial solute-binding protein 3 family. | 0.585 |
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