node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BP1428 | dsbC | BP1428 | BP3270 | Similar to Salmonella typhimurium outer membrane protein OmpH precursor OmpH SW:OMPH_SALTY (P16974) (161 aa) fasta scores: E(): 3.6e-06, 28.84% id in 156 aa, and to Neisseria meningitidis putative outer membrane protein Nma0086 TR:Q9JX30 (EMBL:AL162752) (166 aa) fasta scores: E(): 8.9e-13, 39.63% id in 164 aa; Belongs to the skp family. | Putative thiol:disulphide interchange protein (periplasmic); Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process (By similarity). Necessary for extracellular secretion of the pertussis toxin (PTX); Belongs to the thioredoxin family. DsbC subfamily. | 0.499 |
BP1428 | surA | BP1428 | BP3330 | Similar to Salmonella typhimurium outer membrane protein OmpH precursor OmpH SW:OMPH_SALTY (P16974) (161 aa) fasta scores: E(): 3.6e-06, 28.84% id in 156 aa, and to Neisseria meningitidis putative outer membrane protein Nma0086 TR:Q9JX30 (EMBL:AL162752) (166 aa) fasta scores: E(): 8.9e-13, 39.63% id in 164 aa; Belongs to the skp family. | Putative peptidyl-prolyl cis-trans isomerase; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. | 0.490 |
BP1525 | dsbC | BP1525 | BP3270 | Putative membrane protein; Similar to Agrobacterium tumefaciens Agr_l_2587p TR:AAK89860 (EMBL:AE008329) (171 aa) fasta scores: E(): 0.96, 29.03% id in 155 aa. | Putative thiol:disulphide interchange protein (periplasmic); Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process (By similarity). Necessary for extracellular secretion of the pertussis toxin (PTX); Belongs to the thioredoxin family. DsbC subfamily. | 0.414 |
cbpA | clpB | BP1011 | BP1198 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | 0.804 |
cbpA | cpn10 | BP1011 | BP3496 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.799 |
cbpA | cpn60 | BP1011 | BP3495 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.806 |
cbpA | dnaK | BP1011 | BP2499 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
cbpA | grpE | BP1011 | BP2501 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | Putative GrpE chaperone; 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- [...] | 0.916 |
cbpA | hscA | BP1011 | BP1803 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | Chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.969 |
cbpA | hslO | BP1011 | BP2379 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | Putative 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. | 0.432 |
cbpA | htpG | BP1011 | BP0074 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | tRNA-Leu; Molecular chaperone. Has ATPase activity. | 0.941 |
cbpA | ppiB | BP1011 | BP1906 | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.815 |
clpB | cbpA | BP1198 | BP1011 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. | 0.804 |
clpB | clpX | BP1198 | BP1776 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.600 |
clpB | cpn10 | BP1198 | BP3496 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.827 |
clpB | cpn60 | BP1198 | BP3495 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
clpB | dnaJ | BP1198 | BP2498 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | Molecular chaperone; 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, DnaK [...] | 0.942 |
clpB | dnaK | BP1198 | BP2499 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.987 |
clpB | grpE | BP1198 | BP2501 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | Putative GrpE chaperone; 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- [...] | 0.966 |
clpB | hscA | BP1198 | BP1803 | ATP-dependent protease, ATPase subunit; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] | Chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.922 |