| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AOE40166.1 | groES | BEE12_10100 | BEE12_08960 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.899 |
| AOE40166.1 | groL | BEE12_10100 | BEE12_08965 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.985 |
| AOE40166.1 | grpE_2 | BEE12_10100 | BEE12_02275 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor 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 [...] | 0.993 |
| AOE40166.1 | hslU_1 | BEE12_10100 | BEE12_06210 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.964 |
| AOE40166.1 | hslV | BEE12_10100 | BEE12_06205 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.952 |
| AOE40166.1 | htpG | BEE12_10100 | BEE12_11765 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
| AOE40166.1 | lon_3 | BEE12_10100 | BEE12_11585 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Endopeptidase La; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.933 |
| AOE40166.1 | ybbN | BEE12_10100 | BEE12_11845 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.756 |
| ftsN_1 | hslU_1 | BEE12_06200 | BEE12_06210 | Cell division protein FtsN; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.826 |
| ftsN_1 | hslV | BEE12_06200 | BEE12_06205 | Cell division protein FtsN; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.855 |
| fxsA | hslU_1 | BEE12_08955 | BEE12_06210 | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.510 |
| fxsA | hslV | BEE12_08955 | BEE12_06205 | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.832 |
| fxsA | ybbN | BEE12_08955 | BEE12_11845 | Membrane protein FxsA; F exclusion of bacteriophage T7; overproduction of this protein in Escherichia coli inhibits the F plasmid-mediated exclusion of bacteriophage T7; interacts with the F plasmid-encoded PifA protein; inner membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.713 |
| groES | AOE40166.1 | BEE12_08960 | BEE12_10100 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.899 |
| groES | groL | BEE12_08960 | BEE12_08965 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| groES | grpE_2 | BEE12_08960 | BEE12_02275 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor 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 [...] | 0.988 |
| groES | hslU_1 | BEE12_08960 | BEE12_06210 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.937 |
| groES | hslV | BEE12_08960 | BEE12_06205 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.909 |
| groES | htpG | BEE12_08960 | BEE12_11765 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.924 |
| groES | lon_3 | BEE12_08960 | BEE12_11585 | 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology. | Endopeptidase La; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.518 |