node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Rv2456c | clpX | Rv2456c | Rv2457c | Rv2456c, (MTV008.12c), len: 418 aa. Probable conserved integral membrane transport protein, involved in a efflux system, weakly similar to many e.g. Q9RUR0|YD22_DEIRA|DR1322 putative sugar efflux transporter from Deinococcus radiodurans (389 aa), FASTA scores: opt: 224, E(): 8.4e-06, (24.45% identity in 409 aa overlap); Q9UYY0|PAB0913 multidrug resistance protein from Pyrococcus abyssi (410 aa), FASTA scores: opt: 210, E(): 5.6e-05,(21.8% identity in 408 aa overlap); etc. Contains PS00216 Sugar transport proteins signature 1. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.912 |
Rv2456c | mobA | Rv2456c | Rv2453c | Rv2456c, (MTV008.12c), len: 418 aa. Probable conserved integral membrane transport protein, involved in a efflux system, weakly similar to many e.g. Q9RUR0|YD22_DEIRA|DR1322 putative sugar efflux transporter from Deinococcus radiodurans (389 aa), FASTA scores: opt: 224, E(): 8.4e-06, (24.45% identity in 409 aa overlap); Q9UYY0|PAB0913 multidrug resistance protein from Pyrococcus abyssi (410 aa), FASTA scores: opt: 210, E(): 5.6e-05,(21.8% identity in 408 aa overlap); etc. Contains PS00216 Sugar transport proteins signature 1. | Probable molybdopterin-guanine dinucleotide biosynthesis protein A MobA; Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. | 0.796 |
atpD | clpX | Rv1310 | Rv2457c | Probable ATP synthase beta chain AtpD; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.730 |
atpD | ftsH | Rv1310 | Rv3610c | Probable ATP synthase beta chain AtpD; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Membrane-bound protease FtsH (cell division protein); Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | 0.731 |
atpD | ftsZ | Rv1310 | Rv2150c | Probable ATP synthase beta chain AtpD; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.610 |
atpD | groES | Rv1310 | Rv3418c | Probable ATP synthase beta chain AtpD; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.551 |
clpC1 | clpP1 | Rv3596c | Rv2461c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.997 |
clpC1 | clpP2 | Rv3596c | Rv2460c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.996 |
clpC1 | clpX | Rv3596c | Rv2457c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.822 |
clpC1 | ftsH | Rv3596c | Rv3610c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Membrane-bound protease FtsH (cell division protein); Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | 0.777 |
clpC1 | groES | Rv3596c | Rv3418c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.721 |
clpP1 | clpC1 | Rv2461c | Rv3596c | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | 0.997 |
clpP1 | clpP2 | Rv2461c | Rv2460c | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.999 |
clpP1 | clpX | Rv2461c | Rv2457c | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.998 |
clpP1 | ftsH | Rv2461c | Rv3610c | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | Membrane-bound protease FtsH (cell division protein); Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | 0.866 |
clpP1 | ftsZ | Rv2461c | Rv2150c | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.586 |
clpP1 | groES | Rv2461c | Rv3418c | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.874 |
clpP2 | clpC1 | Rv2460c | Rv3596c | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | 0.996 |
clpP2 | clpP1 | Rv2460c | Rv2461c | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.999 |
clpP2 | clpX | Rv2460c | Rv2457c | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.996 |