| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| corC | cspD | ECA1316 | ECA2659 | Similar to Salmonella typhimurium, and Salmonella typhi magnesium and cobalt efflux protein CorC or stm0667 or sty0712 SWALL:CORC_SALTY (SWALL:Q9R874) (292 aa) fasta scores: E(): 1.5e-92, 85.95% id in 292 aa, and to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri magnesium and cobalt efflux protein CorC or b0658 or c0743 or z0807 or ecs0696 or sf0624 SWALL:CORC_ECOLI (SWALL:P77392) (292 aa) fasta scores: E(): 2.6e-92, 85.61% id in 292 aa. | Cold shock-like protein; Similar to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri cold shock-like protein CspD or CspH or b0880 or c1017 or z1117 or ecs0966 or sf0840 SWALL:CSPD_ECOLI (SWALL:P24245) (74 aa) fasta scores: E(): 9.7e-25, 87.32% id in 71 aa. | 0.574 |
| corC | hslO | ECA1316 | ECA4105 | Similar to Salmonella typhimurium, and Salmonella typhi magnesium and cobalt efflux protein CorC or stm0667 or sty0712 SWALL:CORC_SALTY (SWALL:Q9R874) (292 aa) fasta scores: E(): 1.5e-92, 85.95% id in 292 aa, and to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri magnesium and cobalt efflux protein CorC or b0658 or c0743 or z0807 or ecs0696 or sf0624 SWALL:CORC_ECOLI (SWALL:P77392) (292 aa) fasta scores: E(): 2.6e-92, 85.61% id in 292 aa. | Heat shock protein (33 kDa chaperonin); 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. | 0.724 |
| corC | ptsN | ECA1316 | ECA0286 | Similar to Salmonella typhimurium, and Salmonella typhi magnesium and cobalt efflux protein CorC or stm0667 or sty0712 SWALL:CORC_SALTY (SWALL:Q9R874) (292 aa) fasta scores: E(): 1.5e-92, 85.95% id in 292 aa, and to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri magnesium and cobalt efflux protein CorC or b0658 or c0743 or z0807 or ecs0696 or sf0624 SWALL:CORC_ECOLI (SWALL:P77392) (292 aa) fasta scores: E(): 2.6e-92, 85.61% id in 292 aa. | Similar to Escherichia coli, and Shigella flexneri nitrogen regulatory IIA protein PtsN or RpoP SWALL:PTSN_ECOLI (SWALL:P31222) (163 aa) fasta scores: E(): 1.3e-46, 80.12% id in 156 aa, and to Yersinia pestis phosphotransferase system enzyme IIA PtsN SWALL:AAM83751 (EMBL:AE013615) (164 aa) fasta scores: E(): 6.1e-48, 81.01% id in 158 aa. | 0.667 |
| corC | recB | ECA1316 | ECA0995 | Similar to Salmonella typhimurium, and Salmonella typhi magnesium and cobalt efflux protein CorC or stm0667 or sty0712 SWALL:CORC_SALTY (SWALL:Q9R874) (292 aa) fasta scores: E(): 1.5e-92, 85.95% id in 292 aa, and to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri magnesium and cobalt efflux protein CorC or b0658 or c0743 or z0807 or ecs0696 or sf0624 SWALL:CORC_ECOLI (SWALL:P77392) (292 aa) fasta scores: E(): 2.6e-92, 85.61% id in 292 aa. | Exodeoxyribonuclease V beta chain; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repai [...] | 0.595 |
| cspD | corC | ECA2659 | ECA1316 | Cold shock-like protein; Similar to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri cold shock-like protein CspD or CspH or b0880 or c1017 or z1117 or ecs0966 or sf0840 SWALL:CSPD_ECOLI (SWALL:P24245) (74 aa) fasta scores: E(): 9.7e-25, 87.32% id in 71 aa. | Similar to Salmonella typhimurium, and Salmonella typhi magnesium and cobalt efflux protein CorC or stm0667 or sty0712 SWALL:CORC_SALTY (SWALL:Q9R874) (292 aa) fasta scores: E(): 1.5e-92, 85.95% id in 292 aa, and to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri magnesium and cobalt efflux protein CorC or b0658 or c0743 or z0807 or ecs0696 or sf0624 SWALL:CORC_ECOLI (SWALL:P77392) (292 aa) fasta scores: E(): 2.6e-92, 85.61% id in 292 aa. | 0.574 |
| cspD | hslO | ECA2659 | ECA4105 | Cold shock-like protein; Similar to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri cold shock-like protein CspD or CspH or b0880 or c1017 or z1117 or ecs0966 or sf0840 SWALL:CSPD_ECOLI (SWALL:P24245) (74 aa) fasta scores: E(): 9.7e-25, 87.32% id in 71 aa. | Heat shock protein (33 kDa chaperonin); 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. | 0.612 |
| cspD | ptsN | ECA2659 | ECA0286 | Cold shock-like protein; Similar to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri cold shock-like protein CspD or CspH or b0880 or c1017 or z1117 or ecs0966 or sf0840 SWALL:CSPD_ECOLI (SWALL:P24245) (74 aa) fasta scores: E(): 9.7e-25, 87.32% id in 71 aa. | Similar to Escherichia coli, and Shigella flexneri nitrogen regulatory IIA protein PtsN or RpoP SWALL:PTSN_ECOLI (SWALL:P31222) (163 aa) fasta scores: E(): 1.3e-46, 80.12% id in 156 aa, and to Yersinia pestis phosphotransferase system enzyme IIA PtsN SWALL:AAM83751 (EMBL:AE013615) (164 aa) fasta scores: E(): 6.1e-48, 81.01% id in 158 aa. | 0.613 |
| cspD | recB | ECA2659 | ECA0995 | Cold shock-like protein; Similar to Escherichia coli, Escherichia coli O6, Escherichia coli O157:H7, and Shigella flexneri cold shock-like protein CspD or CspH or b0880 or c1017 or z1117 or ecs0966 or sf0840 SWALL:CSPD_ECOLI (SWALL:P24245) (74 aa) fasta scores: E(): 9.7e-25, 87.32% id in 71 aa. | Exodeoxyribonuclease V beta chain; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repai [...] | 0.507 |
| dnaJ | grpE | ECA3881 | ECA0842 | 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 [...] | Heat shock 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-depen [...] | 0.996 |
| dnaJ | hslO | ECA3881 | ECA4105 | 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 [...] | Heat shock protein (33 kDa chaperonin); 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. | 0.703 |
| dnaJ | hslR | ECA3881 | ECA4104 | 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 [...] | Heat shock protein; Similar to Escherichia coli, Escherichia coli O6, and Escherichia coli O157:H7 heat shock protein 15 HslR or b3400 or c4171 or z4754 or ecs4242 SWALL:HSLR_ECOLI (SWALL:P45802) (133 aa) fasta scores: E(): 2.3e-36, 77.59% id in 125 aa; Belongs to the HSP15 family. | 0.647 |
| dnaJ | hslU | ECA3881 | ECA4262 | 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 [...] | ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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. | 0.969 |
| dnaJ | hslV | ECA3881 | ECA4261 | 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 [...] | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.954 |
| dnaJ | lon | ECA3881 | ECA1150 | 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 [...] | ATP-dependent protease la; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.939 |
| grpE | dnaJ | ECA0842 | ECA3881 | Heat shock 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-depen [...] | 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 [...] | 0.996 |
| grpE | hslO | ECA0842 | ECA4105 | Heat shock 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-depen [...] | Heat shock protein (33 kDa chaperonin); 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. | 0.691 |
| grpE | hslR | ECA0842 | ECA4104 | Heat shock 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-depen [...] | Heat shock protein; Similar to Escherichia coli, Escherichia coli O6, and Escherichia coli O157:H7 heat shock protein 15 HslR or b3400 or c4171 or z4754 or ecs4242 SWALL:HSLR_ECOLI (SWALL:P45802) (133 aa) fasta scores: E(): 2.3e-36, 77.59% id in 125 aa; Belongs to the HSP15 family. | 0.655 |
| grpE | hslU | ECA0842 | ECA4262 | Heat shock 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-depen [...] | ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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. | 0.968 |
| grpE | hslV | ECA0842 | ECA4261 | Heat shock 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-depen [...] | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.962 |
| grpE | lon | ECA0842 | ECA1150 | Heat shock 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-depen [...] | ATP-dependent protease la; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.881 |