node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
aidB | yjfC | b4187 | b4186 | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | 0.552 |
aidB | yjfJ | b4187 | b4182 | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | PspA/IM30 family protein; Putative alpha helical protein; Belongs to the PspA/IM30 family. | 0.420 |
aidB | yjfK | b4187 | b4183 | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | DUF2491 family protein. | 0.509 |
aidB | yjfL | b4187 | b4184 | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | UPF0719 family inner membrane protein. | 0.550 |
aidB | yjfM | b4187 | b4185 | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | DUF1190 family protein. | 0.548 |
gss | yacC | b2988 | b0122 | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | PulS_OutS family protein. | 0.901 |
gss | ygiC | b2988 | b3038 | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | 0.475 |
gss | yjfC | b2988 | b4186 | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | 0.496 |
gss | yjfM | b2988 | b4185 | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | DUF1190 family protein. | 0.401 |
pspA | yjfI | b1304 | b4181 | Regulatory protein for phage-shock-protein operon; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp- specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force. Belongs to the PspA/IM30 family. | DUF2170 family protein. | 0.724 |
pspA | yjfM | b1304 | b4185 | Regulatory protein for phage-shock-protein operon; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp- specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force. Belongs to the PspA/IM30 family. | DUF1190 family protein. | 0.409 |
yacC | gss | b0122 | b2988 | PulS_OutS family protein. | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | 0.901 |
yacC | yjfC | b0122 | b4186 | PulS_OutS family protein. | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | 0.624 |
yacC | yjfM | b0122 | b4185 | PulS_OutS family protein. | DUF1190 family protein. | 0.780 |
ygiC | gss | b3038 | b2988 | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | 0.475 |
ygiC | yjfL | b3038 | b4184 | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | UPF0719 family inner membrane protein. | 0.756 |
ygiC | yjfM | b3038 | b4185 | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | DUF1190 family protein. | 0.815 |
yjfC | aidB | b4186 | b4187 | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | DNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. | 0.552 |
yjfC | gss | b4186 | b2988 | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | 0.496 |
yjfC | yacC | b4186 | b0122 | ATP-Grasp family ATPase; May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Belongs to the glutathionylspermidine synthase preATP-grasp family. | PulS_OutS family protein. | 0.624 |