| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| OPJ56437.1 | secD | CLOTH_08410 | CLOTH_00510 | Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | 0.815 |
| OPJ56437.1 | secF | CLOTH_08410 | CLOTH_00520 | Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | Protein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | 0.814 |
| OPJ56437.1 | secY | CLOTH_08410 | CLOTH_18390 | Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.995 |
| OPJ56437.1 | spoIIAA | CLOTH_08410 | CLOTH_00010 | Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | Anti-sigma F factor antagonist; Belongs to the anti-sigma-factor antagonist family. | 0.888 |
| OPJ56907.1 | spoIIAA | CLOTH_01890 | CLOTH_00010 | Hypothetical protein. | Anti-sigma F factor antagonist; Belongs to the anti-sigma-factor antagonist family. | 0.880 |
| atpE | rpsE | CLOTH_15670 | CLOTH_18420 | ATP synthase subunit c, sodium ion specific; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.805 |
| atpE | secY | CLOTH_15670 | CLOTH_18390 | ATP synthase subunit c, sodium ion specific; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.800 |
| atpE | spoIIAA | CLOTH_15670 | CLOTH_00010 | ATP synthase subunit c, sodium ion specific; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Anti-sigma F factor antagonist; Belongs to the anti-sigma-factor antagonist family. | 0.846 |
| divIB | rpsE | CLOTH_01410 | CLOTH_18420 | Cell division protein DivIB; Essential cell division protein. | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.776 |
| divIB | secY | CLOTH_01410 | CLOTH_18390 | Cell division protein DivIB; Essential cell division protein. | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.886 |
| divIB | spoIIAA | CLOTH_01410 | CLOTH_00010 | Cell division protein DivIB; Essential cell division protein. | Anti-sigma F factor antagonist; Belongs to the anti-sigma-factor antagonist family. | 0.778 |
| rpsE | atpE | CLOTH_18420 | CLOTH_15670 | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | ATP synthase subunit c, sodium ion specific; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.805 |
| rpsE | divIB | CLOTH_18420 | CLOTH_01410 | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | Cell division protein DivIB; Essential cell division protein. | 0.776 |
| rpsE | secY | CLOTH_18420 | CLOTH_18390 | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.999 |
| rpsE | spoIIAA | CLOTH_18420 | CLOTH_00010 | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | Anti-sigma F factor antagonist; Belongs to the anti-sigma-factor antagonist family. | 0.830 |
| secD | OPJ56437.1 | CLOTH_00510 | CLOTH_08410 | Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | 0.815 |
| secD | secF | CLOTH_00510 | CLOTH_00520 | Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | Protein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | 0.997 |
| secD | secY | CLOTH_00510 | CLOTH_18390 | Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.932 |
| secD | spoIIAA | CLOTH_00510 | CLOTH_00010 | Protein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | Anti-sigma F factor antagonist; Belongs to the anti-sigma-factor antagonist family. | 0.837 |
| secF | OPJ56437.1 | CLOTH_00520 | CLOTH_08410 | Protein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. | Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. | 0.814 |
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