| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MMAR_1007 | MMAR_1611 | MMAR_1007 | MMAR_1611 | Transcriptional regulator. | Transcriptional regulatory protein; Involved in transcriptional mechanism. | 0.692 |
| MMAR_1007 | MMAR_3267 | MMAR_1007 | MMAR_3267 | Transcriptional regulator. | Conserved transmembrane protein. | 0.452 |
| MMAR_1007 | MMAR_4918 | MMAR_1007 | MMAR_4918 | Transcriptional regulator. | Conserved protein; Contains transcriptional regulatory domain. | 0.429 |
| MMAR_1007 | MMAR_5035 | MMAR_1007 | MMAR_5035 | Transcriptional regulator. | Conserved hypothetical protein; Function unknown; contains a FMN-binding split barrel domain. possible role in the electron-transfer pathway. the FMN-binding split barrel is related to the ferredoxin reductase-like FAD-binding domain. flavodoxins are an example of a group of proteins with a tightly bound flavin mononucleotide (FMN) that mediate electron transfer at low redox potential. | 0.477 |
| MMAR_1007 | atpE | MMAR_1007 | MMAR_4092 | Transcriptional regulator. | ATP synthase C chain AtpE; 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. | 0.608 |
| MMAR_1007 | mmpL5 | MMAR_1007 | MMAR_1005 | Transcriptional regulator. | Conserved transmembrane transport protein, MmpL5; Thought to be involved in fatty acid transport. | 0.879 |
| MMAR_1007 | mmpS5 | MMAR_1007 | MMAR_1006 | Transcriptional regulator. | Conserved transmembrane proteinm, MmpS5. | 0.883 |
| MMAR_1007 | pepQ | MMAR_1007 | MMAR_2180 | Transcriptional regulator. | Cytoplasmic peptidase PepQ; Function unknown, hydrolyses peptides. | 0.608 |
| MMAR_1611 | MMAR_1007 | MMAR_1611 | MMAR_1007 | Transcriptional regulatory protein; Involved in transcriptional mechanism. | Transcriptional regulator. | 0.692 |
| MMAR_1611 | MMAR_4918 | MMAR_1611 | MMAR_4918 | Transcriptional regulatory protein; Involved in transcriptional mechanism. | Conserved protein; Contains transcriptional regulatory domain. | 0.737 |
| MMAR_3267 | MMAR_1007 | MMAR_3267 | MMAR_1007 | Conserved transmembrane protein. | Transcriptional regulator. | 0.452 |
| MMAR_4918 | MMAR_1007 | MMAR_4918 | MMAR_1007 | Conserved protein; Contains transcriptional regulatory domain. | Transcriptional regulator. | 0.429 |
| MMAR_4918 | MMAR_1611 | MMAR_4918 | MMAR_1611 | Conserved protein; Contains transcriptional regulatory domain. | Transcriptional regulatory protein; Involved in transcriptional mechanism. | 0.737 |
| MMAR_5035 | MMAR_1007 | MMAR_5035 | MMAR_1007 | Conserved hypothetical protein; Function unknown; contains a FMN-binding split barrel domain. possible role in the electron-transfer pathway. the FMN-binding split barrel is related to the ferredoxin reductase-like FAD-binding domain. flavodoxins are an example of a group of proteins with a tightly bound flavin mononucleotide (FMN) that mediate electron transfer at low redox potential. | Transcriptional regulator. | 0.477 |
| atpE | MMAR_1007 | MMAR_4092 | MMAR_1007 | ATP synthase C chain AtpE; 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. | Transcriptional regulator. | 0.608 |
| atpE | mmpL5 | MMAR_4092 | MMAR_1005 | ATP synthase C chain AtpE; 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. | Conserved transmembrane transport protein, MmpL5; Thought to be involved in fatty acid transport. | 0.672 |
| atpE | mmpS5 | MMAR_4092 | MMAR_1006 | ATP synthase C chain AtpE; 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. | Conserved transmembrane proteinm, MmpS5. | 0.637 |
| atpE | pepQ | MMAR_4092 | MMAR_2180 | ATP synthase C chain AtpE; 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. | Cytoplasmic peptidase PepQ; Function unknown, hydrolyses peptides. | 0.902 |
| mmpL5 | MMAR_1007 | MMAR_1005 | MMAR_1007 | Conserved transmembrane transport protein, MmpL5; Thought to be involved in fatty acid transport. | Transcriptional regulator. | 0.879 |
| mmpL5 | atpE | MMAR_1005 | MMAR_4092 | Conserved transmembrane transport protein, MmpL5; Thought to be involved in fatty acid transport. | ATP synthase C chain AtpE; 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. | 0.672 |