node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cpxR | dsbA | b3912 | b3860 | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | 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. | 0.644 |
cpxR | spy | b3912 | b1743 | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | 0.757 |
cpxR | srkA | b3912 | b3859 | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | 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. | 0.487 |
cpxR | yccA | b3912 | b0970 | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | Modulator of FtsH protease, inner membrane protein; Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed; Belongs to the BI1 family. | 0.559 |
cpxR | yebE | b3912 | b1846 | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | DUF533 family inner membrane protein. | 0.447 |
dsbA | cpxR | b3860 | b3912 | 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. | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | 0.644 |
dsbA | spy | b3860 | b1743 | 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 ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | 0.449 |
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 | 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 |
dsbA | yihF | b3860 | b3861 | 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. | DUF945 family protein; Putative GTP-binding protein; To E.coli YdgA and H.influenzae HI_1236. | 0.472 |
ldtC | spy | b1113 | b1743 | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | 0.986 |
ldtC | srkA | b1113 | b3859 | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. | 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. | 0.486 |
ldtC | yccA | b1113 | b0970 | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. | Modulator of FtsH protease, inner membrane protein; Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed; Belongs to the BI1 family. | 0.627 |
ldtC | yebE | b1113 | b1846 | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. | DUF533 family inner membrane protein. | 0.984 |
modE | srkA | b0761 | b3859 | Transcriptional repressor for the molybdenum transport operon modABC; Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate. Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity. Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate. The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3'. Acts as a regulator of the expression of 6 [...] | 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. | 0.427 |
spy | cpxR | b1743 | b3912 | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | Response regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] | 0.757 |
spy | dsbA | b1743 | b3860 | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | 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. | 0.449 |
spy | ldtC | b1743 | b1113 | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. | 0.986 |
spy | srkA | b1743 | b3859 | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | 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. | 0.449 |
spy | yccA | b1743 | b0970 | Periplasmic ATP-independent protein refolding chaperone, stress-induced; An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic prote [...] | Modulator of FtsH protease, inner membrane protein; Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed; Belongs to the BI1 family. | 0.679 |