node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABK70762.1 | esxA | MSMEG_0064 | MSMEG_0066 | Ppe family protein; Identified by match to protein family HMM PF00823. | Early secretory antigenic target, 6 kDa; An exported protein. Unlike its M.tuberculosis counterpart has poor pore forming ability in artificial liposomes, does not undergo conformational change at acidic pH. Mutation of 2 residues to those found in M.tuberculosis (25-TA-26 to IH) alters the properties of this protein so that it inserts into liposomes at acidic pH, forming pores, like its M.tuberculosis counterpart. | 0.866 |
ABK70762.1 | pE | MSMEG_0064 | MSMEG_0412 | Ppe family protein; Identified by match to protein family HMM PF00823. | Conserved hypothetical protein. | 0.585 |
ABK70862.1 | lprG | MSMEG_3662 | MSMEG_3070 | Mannose-binding lectin; Identified by match to protein family HMM PF01453; match to protein family HMM PF01476. | LprG protein; Probably helps membrane protein MSMEG_3069/MSMEI_2992 (P55) transport triacylglycerides (TAG) across the inner cell membrane into the periplasm and probably ultimately to the outer membrane (By similarity). Required for MSMEG_3069/MSMEI_2992 export activity. Export of ethidium bromide by MSMEG_3069/MSMEI_2992 can be complemented by the equivalent operon from M.tuberculosis (lprG-Rv1410c). Belongs to the LppX/LprAFG lipoprotein family. | 0.405 |
ABK70912.1 | pE | MSMEG_0619 | MSMEG_0412 | Ppe family protein; Identified by match to protein family HMM PF00823. | Conserved hypothetical protein. | 0.584 |
ABK74738.1 | pE | MSMEG_2737 | MSMEG_0412 | Ppe family protein. | Conserved hypothetical protein. | 0.589 |
dnaK | groL | MSMEG_0709 | MSMEG_0880 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.992 |
dnaK | groS | MSMEG_0709 | MSMEG_1582 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.986 |
esxA | ABK70762.1 | MSMEG_0066 | MSMEG_0064 | Early secretory antigenic target, 6 kDa; An exported protein. Unlike its M.tuberculosis counterpart has poor pore forming ability in artificial liposomes, does not undergo conformational change at acidic pH. Mutation of 2 residues to those found in M.tuberculosis (25-TA-26 to IH) alters the properties of this protein so that it inserts into liposomes at acidic pH, forming pores, like its M.tuberculosis counterpart. | Ppe family protein; Identified by match to protein family HMM PF00823. | 0.866 |
esxA | groL | MSMEG_0066 | MSMEG_0880 | Early secretory antigenic target, 6 kDa; An exported protein. Unlike its M.tuberculosis counterpart has poor pore forming ability in artificial liposomes, does not undergo conformational change at acidic pH. Mutation of 2 residues to those found in M.tuberculosis (25-TA-26 to IH) alters the properties of this protein so that it inserts into liposomes at acidic pH, forming pores, like its M.tuberculosis counterpart. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.864 |
esxA | groS | MSMEG_0066 | MSMEG_1582 | Early secretory antigenic target, 6 kDa; An exported protein. Unlike its M.tuberculosis counterpart has poor pore forming ability in artificial liposomes, does not undergo conformational change at acidic pH. Mutation of 2 residues to those found in M.tuberculosis (25-TA-26 to IH) alters the properties of this protein so that it inserts into liposomes at acidic pH, forming pores, like its M.tuberculosis counterpart. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.473 |
groL | dnaK | MSMEG_0880 | MSMEG_0709 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
groL | esxA | MSMEG_0880 | MSMEG_0066 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Early secretory antigenic target, 6 kDa; An exported protein. Unlike its M.tuberculosis counterpart has poor pore forming ability in artificial liposomes, does not undergo conformational change at acidic pH. Mutation of 2 residues to those found in M.tuberculosis (25-TA-26 to IH) alters the properties of this protein so that it inserts into liposomes at acidic pH, forming pores, like its M.tuberculosis counterpart. | 0.864 |
groL | groS | MSMEG_0880 | MSMEG_1582 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
groL | katG | MSMEG_0880 | MSMEG_3461 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Catalase/peroxidase HPI; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. | 0.400 |
groL | katG-2 | MSMEG_0880 | MSMEG_3729 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Catalase/peroxidase HPI; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily. | 0.409 |
groS | dnaK | MSMEG_1582 | MSMEG_0709 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.986 |
groS | esxA | MSMEG_1582 | MSMEG_0066 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Early secretory antigenic target, 6 kDa; An exported protein. Unlike its M.tuberculosis counterpart has poor pore forming ability in artificial liposomes, does not undergo conformational change at acidic pH. Mutation of 2 residues to those found in M.tuberculosis (25-TA-26 to IH) alters the properties of this protein so that it inserts into liposomes at acidic pH, forming pores, like its M.tuberculosis counterpart. | 0.473 |
groS | groL | MSMEG_1582 | MSMEG_0880 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
groS | katG | MSMEG_1582 | MSMEG_3461 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Catalase/peroxidase HPI; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. | 0.418 |
groS | katG-2 | MSMEG_1582 | MSMEG_3729 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Catalase/peroxidase HPI; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily. | 0.423 |