node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
fetA | fetB | b0490 | b0491 | Iron export ABC transporter ATPase; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for energy coupling to the transport system. | Iron export ABC transporter permease; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane; Belongs to the UPF0014 family. | 0.998 |
fetA | qmcA | b0490 | b0489 | Iron export ABC transporter ATPase; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for energy coupling to the transport system. | PHB domain membrane-anchored putative protease; Identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant. May play a role in the quality control of integral membrane proteins; Belongs to the band 7/mec-2 family. | 0.837 |
fetA | ybbJ | b0490 | b0488 | Iron export ABC transporter ATPase; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for energy coupling to the transport system. | Inner membrane protein; stimulator of the QmcA suppressor of ftsH-htpX. | 0.731 |
fetB | fetA | b0491 | b0490 | Iron export ABC transporter permease; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane; Belongs to the UPF0014 family. | Iron export ABC transporter ATPase; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for energy coupling to the transport system. | 0.998 |
fetB | qmcA | b0491 | b0489 | Iron export ABC transporter permease; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane; Belongs to the UPF0014 family. | PHB domain membrane-anchored putative protease; Identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant. May play a role in the quality control of integral membrane proteins; Belongs to the band 7/mec-2 family. | 0.667 |
fetB | ybbJ | b0491 | b0488 | Iron export ABC transporter permease; Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane; Belongs to the UPF0014 family. | Inner membrane protein; stimulator of the QmcA suppressor of ftsH-htpX. | 0.772 |
ftsH | hflC | b3178 | b4175 | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | 0.999 |
ftsH | hflK | b3178 | b4174 | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | Modulator for HflB protease specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflK subfamily. | 0.999 |
ftsH | htpX | b3178 | b1829 | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | 0.905 |
ftsH | qmcA | b3178 | b0489 | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | PHB domain membrane-anchored putative protease; Identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant. May play a role in the quality control of integral membrane proteins; Belongs to the band 7/mec-2 family. | 0.882 |
hflC | ftsH | b4175 | b3178 | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | 0.999 |
hflC | hflK | b4175 | b4174 | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | Modulator for HflB protease specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflK subfamily. | 0.999 |
hflC | htpX | b4175 | b1829 | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | 0.440 |
hflC | qmcA | b4175 | b0489 | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | PHB domain membrane-anchored putative protease; Identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant. May play a role in the quality control of integral membrane proteins; Belongs to the band 7/mec-2 family. | 0.520 |
hflC | ybbJ | b4175 | b0488 | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | Inner membrane protein; stimulator of the QmcA suppressor of ftsH-htpX. | 0.563 |
hflC | yqiK | b4175 | b3051 | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | PHB family membrane protein, function unknown; Putative membrane protein. | 0.664 |
hflK | ftsH | b4174 | b3178 | Modulator for HflB protease specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflK subfamily. | Protease, ATP-dependent zinc-metallo; 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] | 0.999 |
hflK | hflC | b4174 | b4175 | Modulator for HflB protease specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflK subfamily. | HflB protease modulator specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflC subfamily. | 0.999 |
hflK | htpX | b4174 | b1829 | Modulator for HflB protease specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflK subfamily. | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. | 0.515 |
hflK | qmcA | b4174 | b0489 | Modulator for HflB protease specific for phage lambda cII repressor; HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. Belongs to the band 7/mec-2 family. HflK subfamily. | PHB domain membrane-anchored putative protease; Identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant. May play a role in the quality control of integral membrane proteins; Belongs to the band 7/mec-2 family. | 0.598 |