node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dinB | dnaE | b0231 | b0184 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | 0.902 |
dinB | dnaN | b0231 | b3701 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | 0.999 |
dinB | dnaQ | b0231 | b0215 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase III epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction. | 0.685 |
dinB | dnaX | b0231 | b0470 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase III/DNA elongation factor III, tau and gamma subunits; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open [...] | 0.684 |
dinB | hda | b0231 | b2496 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | ATPase regulatory factor involved in DnaA inactivation; Mediates the interactions of DNA replication initiator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinitiation, a process called regulatory inhibition of DnaA or RIDA. ADP-binding activates Hda to hydrolyze DnaA-ATP; Hda monomers bind to ADP with about 200-fold greater affinity than for ATP. RIDA function can be genetically separated from viability, suggesting this protein has another function as well. | 0.563 |
dinB | holB | b0231 | b1099 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase III, delta prime subunit; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Pr [...] | 0.690 |
dinB | polB | b0231 | b0060 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | DNA polymerase II; Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader. | 0.994 |
dinB | umuC | b0231 | b1184 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | Translesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp- complex may target Pol V to replication co [...] | 0.721 |
dnaA | dnaE | b3702 | b0184 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | 0.965 |
dnaA | dnaN | b3702 | b3701 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | 0.999 |
dnaA | dnaQ | b3702 | b0215 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | DNA polymerase III epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction. | 0.822 |
dnaA | dnaX | b3702 | b0470 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | DNA polymerase III/DNA elongation factor III, tau and gamma subunits; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open [...] | 0.955 |
dnaA | hda | b3702 | b2496 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | ATPase regulatory factor involved in DnaA inactivation; Mediates the interactions of DNA replication initiator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinitiation, a process called regulatory inhibition of DnaA or RIDA. ADP-binding activates Hda to hydrolyze DnaA-ATP; Hda monomers bind to ADP with about 200-fold greater affinity than for ATP. RIDA function can be genetically separated from viability, suggesting this protein has another function as well. | 0.962 |
dnaA | holA | b3702 | b0640 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | DNA polymerase III, delta subunit; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The delta subunit is the wrench that will open the beta subunit dimer, which has been modeled to leave a gap large enough for ssDNA to pass through. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers [...] | 0.745 |
dnaA | holB | b3702 | b1099 | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | DNA polymerase III, delta prime subunit; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Pr [...] | 0.771 |
dnaE | dinB | b0184 | b0231 | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by Pol IV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of Pol IV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long- term survival and evol [...] | 0.902 |
dnaE | dnaA | b0184 | b3702 | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | Chromosomal replication initiator protein DnaA, DNA-binding transcriptional dual regulator; Plays a key role in the initiation and regulation of chromosomal replication. Binds in an ATP-dependent fashion to the origin of replication (oriC) to initiate formation of the DNA replication initiation complex exactly once per cell cycle. Binds the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3'); subsequent binding of DNA polymerase III subunits leads to replisome formation. The DnaA- ATP form converts to DnaA-ADP; once converted to ADP the protein cannot initiate replication, ensuring onl [...] | 0.965 |
dnaE | dnaN | b0184 | b3701 | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...] | 0.999 |
dnaE | dnaQ | b0184 | b0215 | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | DNA polymerase III epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction. | 0.999 |
dnaE | dnaX | b0184 | b0470 | DNA polymerase III alpha subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius. | DNA polymerase III/DNA elongation factor III, tau and gamma subunits; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open [...] | 0.999 |