node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
degP | dsbA | b0161 | b3860 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | 0.908 |
degP | dsbB | b0161 | b1185 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | 0.580 |
degP | dsbC | b0161 | b2893 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.578 |
degP | phoA | b0161 | b0383 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | Alkaline phosphatase; start codon corrected; Protein involved in phosphorus metabolic process; Belongs to the alkaline phosphatase family. | 0.543 |
degP | surA | b0161 | b0053 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. 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. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. | 0.947 |
dsbA | degP | b3860 | b0161 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | 0.908 |
dsbA | dsbB | b3860 | b1185 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | 0.999 |
dsbA | dsbC | b3860 | b2893 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.983 |
dsbA | dsbD | b3860 | b4136 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. | 0.963 |
dsbA | dsbE | b3860 | b2195 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Periplasmic thioredoxin of cytochrome c-type biogenesis; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD. | 0.959 |
dsbA | dsbG | b3860 | b0604 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Thiol:disulfide interchange protein, periplasmic; Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro. Belongs to the thioredoxin family. DsbC subfamily. | 0.908 |
dsbA | phoA | b3860 | b0383 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Alkaline phosphatase; start codon corrected; Protein involved in phosphorus metabolic process; Belongs to the alkaline phosphatase family. | 0.906 |
dsbA | srkA | b3860 | b3859 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Cpx stress response Thr/Ser protein kinase; A protein kinase that (auto)phosphorylates on Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Protects cells from stress by antagonizing the MazE-MazF TA module, probably indirectly as it has not been seen to phosphorylate MazE, MazF or MazG. Probably involved in the extracytoplasmic stress response. | 0.980 |
dsbA | surA | b3860 | b0053 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. 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. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. | 0.937 |
dsbA | yihD | b3860 | b3858 | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | DUF1040 protein YihD; To H.influenzae HI_0845. | 0.951 |
dsbB | degP | b1185 | b0161 | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | 0.580 |
dsbB | dsbA | b1185 | b3860 | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. | 0.999 |
dsbB | dsbC | b1185 | b2893 | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.970 |
dsbB | dsbD | b1185 | b4136 | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. | 0.980 |
dsbB | dsbE | b1185 | b2195 | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. | Periplasmic thioredoxin of cytochrome c-type biogenesis; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD. | 0.952 |