| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MMAR_2575 | MMAR_3113 | MMAR_2575 | MMAR_3113 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | Conserved hypothetical protein. | 0.546 |
| MMAR_2575 | MMAR_3547 | MMAR_2575 | MMAR_3547 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | 0.534 |
| MMAR_2575 | alaS | MMAR_2575 | MMAR_2170 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | alanyl-tRNA synthetase AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.566 |
| MMAR_2575 | ppiA | MMAR_2575 | MMAR_0011 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | Peptidyl-prolyl cis-trans isomerase A, PpiA; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.536 |
| MMAR_2575 | ppiB | MMAR_2575 | MMAR_2125 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | Peptidyl-prolyl cis-trans isomerase B PpiB; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.536 |
| MMAR_2575 | rplC | MMAR_2575 | MMAR_1031 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 50S ribosomal protein L3 RplC; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family. | 0.543 |
| MMAR_2575 | rplJ | MMAR_2575 | MMAR_0990 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 50S ribosomal protein L10, RplJ; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family. | 0.563 |
| MMAR_2575 | rplN | MMAR_2575 | MMAR_1045 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 50S ribosomal protein L14, RplN; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.537 |
| MMAR_2575 | rplW | MMAR_2575 | MMAR_1033 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 50S ribosomal protein L23, RplW; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family. | 0.541 |
| MMAR_2575 | rpmD | MMAR_2575 | MMAR_1053 | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 50S ribosomal protein L30, RpmD. | 0.604 |
| MMAR_3113 | MMAR_2575 | MMAR_3113 | MMAR_2575 | Conserved hypothetical protein. | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 0.546 |
| MMAR_3547 | MMAR_2575 | MMAR_3547 | MMAR_2575 | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 0.534 |
| MMAR_3547 | alaS | MMAR_3547 | MMAR_2170 | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | alanyl-tRNA synthetase AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.616 |
| MMAR_3547 | ppiA | MMAR_3547 | MMAR_0011 | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | Peptidyl-prolyl cis-trans isomerase A, PpiA; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.483 |
| MMAR_3547 | ppiB | MMAR_3547 | MMAR_2125 | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | Peptidyl-prolyl cis-trans isomerase B PpiB; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.462 |
| alaS | MMAR_2575 | MMAR_2170 | MMAR_2575 | alanyl-tRNA synthetase AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 0.566 |
| alaS | MMAR_3547 | MMAR_2170 | MMAR_3547 | alanyl-tRNA synthetase AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | 0.616 |
| ppiA | MMAR_2575 | MMAR_0011 | MMAR_2575 | Peptidyl-prolyl cis-trans isomerase A, PpiA; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PE-PGRS family protein; Function unknown. seems to influence both cell surface interactions among mycobacteria and the interactions of bacteria with macrophages. | 0.536 |
| ppiA | MMAR_3547 | MMAR_0011 | MMAR_3547 | Peptidyl-prolyl cis-trans isomerase A, PpiA; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Serine/threonine-protein kinase transcriptional regulatory protein; Involved in signal transduction (via phosphorylation). involved in transcriptional regulatory mechanism and in the regulation of secondary metabolites [catalytic activity: ATP + a protein = ADP + a phosphoprotein]. N-term resembles PknK from MTB. | 0.483 |
| ppiA | rplC | MMAR_0011 | MMAR_1031 | Peptidyl-prolyl cis-trans isomerase A, PpiA; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 50S ribosomal protein L3 RplC; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family. | 0.801 |