node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
gspO | lepA | b3335 | b2569 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | 0.627 |
gspO | lepB | b3335 | b2568 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | 0.919 |
gspO | lspA | b3335 | b0027 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Prolipoprotein signal peptidase (signal peptidase II); This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | 0.638 |
gspO | ompA | b3335 | b0957 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Outer membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...] | 0.624 |
gspO | secA | b3335 | b0098 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Preprotein translocase subunit, ATPase; Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | 0.678 |
gspO | secY | b3335 | b3300 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Preprotein translocase membrane subunit; 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. SecY is r [...] | 0.780 |
gspO | yidC | b3335 | b3705 | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | Membrane protein insertase; Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec- independent subunit c of the F(0)ATP synthase, M13 phage procoat and the N-terminus of leade [...] | 0.804 |
lepA | gspO | b2569 | b3335 | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | 0.627 |
lepA | lepB | b2569 | b2568 | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | 0.996 |
lepA | rnc | b2569 | b2567 | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | RNase III; Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, showing s [...] | 0.749 |
lepA | secA | b2569 | b0098 | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | Preprotein translocase subunit, ATPase; Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | 0.494 |
lepA | secY | b2569 | b3300 | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | Preprotein translocase membrane subunit; 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. SecY is r [...] | 0.447 |
lepA | yidC | b2569 | b3705 | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | Membrane protein insertase; Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec- independent subunit c of the F(0)ATP synthase, M13 phage procoat and the N-terminus of leade [...] | 0.443 |
lepB | gspO | b2568 | b3335 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. | 0.919 |
lepB | lepA | b2568 | b2569 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...] | 0.996 |
lepB | lspA | b2568 | b0027 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | Prolipoprotein signal peptidase (signal peptidase II); This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | 0.939 |
lepB | ompA | b2568 | b0957 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | Outer membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...] | 0.930 |
lepB | rnc | b2568 | b2567 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | RNase III; Digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. Involved in the processing of rRNA precursors, viral transcripts, some mRNAs and at least 1 tRNA (metY, a minor form of tRNA-init-Met). Cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs; cleavage can occur in assembled 30S, 50S and even 70S subunits and is influenced by the presence of ribosomal proteins. The E.coli enzyme does not cleave R.capsulatus rRNA precursor, although R.capsulatus will complement an E.coli disruption, showing s [...] | 0.976 |
lepB | secA | b2568 | b0098 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | Preprotein translocase subunit, ATPase; Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | 0.920 |
lepB | secY | b2568 | b3300 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | Preprotein translocase membrane subunit; 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. SecY is r [...] | 0.943 |