node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
aroA | cmk | b0908 | b0910 | 5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.948 |
aroA | rpsA | b0908 | b0911 | 5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | 0.430 |
aroA | ycaL | b0908 | b0909 | 5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.462 |
bepA | degP | b2494 | b0161 | OM protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions; Belongs to the peptidase M48 family. BepA subfamily. | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | 0.720 |
bepA | ycaL | b2494 | b0909 | OM protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions; Belongs to the peptidase M48 family. BepA subfamily. | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.949 |
cmk | aroA | b0910 | b0908 | Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Belongs to the cytidylate kinase family. Type 1 subfamily. | 5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | 0.948 |
cmk | rpsA | b0910 | b0911 | Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Belongs to the cytidylate kinase family. Type 1 subfamily. | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | 0.985 |
cmk | ycaL | b0910 | b0909 | Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Belongs to the cytidylate kinase family. Type 1 subfamily. | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.558 |
crfC | ycaL | b4109 | b0909 | Clamp-binding sister replication fork colocalization protein, dynamin-related; Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.412 |
degP | bepA | b0161 | b2494 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | OM protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions; Belongs to the peptidase M48 family. BepA subfamily. | 0.720 |
degP | ftsH | b0161 | b3178 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | 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 [...] | 0.790 |
degP | ycaL | b0161 | b0909 | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.453 |
ftsH | degP | b3178 | b0161 | 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 [...] | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] | 0.790 |
ftsH | rpsA | b3178 | b0911 | 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 [...] | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | 0.698 |
ftsH | ycaL | b3178 | b0909 | 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 peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.428 |
lit | ycaL | b1139 | b0909 | T4 phage exclusion protein; Interacts with a short DNA sequence about one-quarter of the way into the major capsid protein gene 23 of T4; general translation inhibition occurs when this late gene of the virus is expressed. Belongs to the peptidase U49 family. | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.457 |
rpsA | aroA | b0911 | b0908 | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | 5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | 0.430 |
rpsA | cmk | b0911 | b0910 | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Belongs to the cytidylate kinase family. Type 1 subfamily. | 0.985 |
rpsA | ftsH | b0911 | b3178 | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | 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 [...] | 0.698 |
rpsA | ycaL | b0911 | b0909 | 30S ribosomal subunit protein S1; Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translat [...] | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. | 0.419 |