dinP protein (Streptococcus mitis) - STRING interaction network

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dinP

DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. (353 aa)

Predicted Functional Partners:

dnaN

0.894

recA

0.756

smi_1367

0.566

polI

0.563

dnaE

0.519

pfl

0.506

dinG

0.457

recN

0.457

rodA

0.446

ftsW

0.446

Your Current Organism:

Streptococcus mitis

NCBI taxonomy Id: 365659
Other names: S. mitis B6, Streptococcus mitis B6, Streptococcus mitis str. B6, Streptococcus mitis strain B6

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
dinG	dinP	smi_0855	smi_1816	ATP-dependent helicase DinG; 3'-5' exonuclease.	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.457
dinG	dnaE	smi_0855	smi_1003	ATP-dependent helicase DinG; 3'-5' exonuclease.	DNA-polymerase III alpha-chain.	0.564
dinG	dnaN	smi_0855	smi_0002	ATP-dependent helicase DinG; 3'-5' exonuclease.	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. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	0.968
dinG	polI	smi_0855	smi_0048	ATP-dependent helicase DinG; 3'-5' exonuclease.	DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.	0.981
dinG	recA	smi_0855	smi_1839	ATP-dependent helicase DinG; 3'-5' exonuclease.	RecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.	0.771
dinG	recN	smi_0855	smi_1019	ATP-dependent helicase DinG; 3'-5' exonuclease.	DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.	0.401
dinG	rodA	smi_0855	smi_0856	ATP-dependent helicase DinG; 3'-5' exonuclease.	Pfam01098, FTSW_RODA_SPOVE, cell cycle protein; Belongs to the SEDS family.	0.803
dinG	smi_1367	smi_0855	smi_1367	ATP-dependent helicase DinG; 3'-5' exonuclease.	cI-like repressor, S. pneumoniae bacteriophage EJ-1; COG2932, predicted transcriptional regulator.	0.644
dinP	dinG	smi_1816	smi_0855	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	ATP-dependent helicase DinG; 3'-5' exonuclease.	0.457
dinP	dnaE	smi_1816	smi_1003	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	DNA-polymerase III alpha-chain.	0.519
dinP	dnaN	smi_1816	smi_0002	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	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. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]	0.894
dinP	ftsW	smi_1816	smi_0984	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	Cell division protein FtsW; Belongs to the SEDS family.	0.446
dinP	pfl	smi_1816	smi_1815	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	Pyruvate formate-lyase.	0.506
dinP	polI	smi_1816	smi_0048	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.	0.563
dinP	recA	smi_1816	smi_1839	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	RecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.	0.756
dinP	recN	smi_1816	smi_1019	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.	0.457
dinP	rodA	smi_1816	smi_0856	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	Pfam01098, FTSW_RODA_SPOVE, cell cycle protein; Belongs to the SEDS family.	0.446
dinP	smi_1367	smi_1816	smi_1367	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	cI-like repressor, S. pneumoniae bacteriophage EJ-1; COG2932, predicted transcriptional regulator.	0.566
dnaE	dinG	smi_1003	smi_0855	DNA-polymerase III alpha-chain.	ATP-dependent helicase DinG; 3'-5' exonuclease.	0.564
dnaE	dinP	smi_1003	smi_1816	DNA-polymerase III alpha-chain.	DNA-damage-inducible protein P; Poorly processive, error-prone DNA polymerase involved in 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 PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.519

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