Meso_0210 protein (Chelativorans sp. BNC1) - STRING interaction network

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Your Current Organism:

Chelativorans sp. BNC1

NCBI taxonomy Id: 266779
Other names: C. sp. BNC1, Mesorhizobium sp. BNC1

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Meso_0002	Meso_0210	Meso_0002	Meso_0210	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 [...]	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	0.700
Meso_0002	Meso_1582	Meso_0002	Meso_1582	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 [...]	TIGRFAM: DNA polymerase III, delta prime subunit; KEGG: mlo:mll0423 DNA polymerase III, delta prime subunit.	0.998
Meso_0002	Meso_2226	Meso_0002	Meso_2226	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 [...]	DNA polymerase III, epsilon subunit; KEGG: mag:amb1544 predicted signal-transduction protein containing cAMP-binding and CBS domains; TIGRFAM: DNA polymerase III, epsilon subunit; PFAM: CBS domain containing protein Exonuclease, RNase T and DNA polymerase III; SMART: Exonuclease.	0.992
Meso_0002	Meso_3317	Meso_0002	Meso_3317	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 [...]	TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III, delta; KEGG: mlo:mlr4475 putative DNA polymerase III, delta subunit.	0.998
Meso_0002	dinB	Meso_0002	Meso_1344	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 [...]	UMUC-like DNA-repair protein; 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.	0.882
Meso_0002	dnaQ	Meso_0002	Meso_3482	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 [...]	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.	0.994
Meso_0002	recA	Meso_0002	Meso_1263	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 [...]	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.	0.914
Meso_0002	ruvA	Meso_0002	Meso_3178	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 [...]	Holliday junction DNA helicase subunit RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.	0.453
Meso_0210	Meso_0002	Meso_0210	Meso_0002	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	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 [...]	0.700
Meso_0210	Meso_0211	Meso_0210	Meso_0211	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	Hypothetical protein.	0.773
Meso_0210	Meso_1582	Meso_0210	Meso_1582	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	TIGRFAM: DNA polymerase III, delta prime subunit; KEGG: mlo:mll0423 DNA polymerase III, delta prime subunit.	0.631
Meso_0210	Meso_2226	Meso_0210	Meso_2226	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	DNA polymerase III, epsilon subunit; KEGG: mag:amb1544 predicted signal-transduction protein containing cAMP-binding and CBS domains; TIGRFAM: DNA polymerase III, epsilon subunit; PFAM: CBS domain containing protein Exonuclease, RNase T and DNA polymerase III; SMART: Exonuclease.	0.651
Meso_0210	Meso_3317	Meso_0210	Meso_3317	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	TIGRFAM: DNA polymerase III, delta subunit; PFAM: DNA polymerase III, delta; KEGG: mlo:mlr4475 putative DNA polymerase III, delta subunit.	0.697
Meso_0210	Meso_3581	Meso_0210	Meso_3581	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	DNA helicase/exodeoxyribonuclease V, subunit A; PFAM: UvrD/REP helicase; KEGG: mlo:mll5083 ATP-dependent nuclease subunit A; Belongs to the helicase family. UvrD subfamily.	0.721
Meso_0210	dinB	Meso_0210	Meso_1344	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	UMUC-like DNA-repair protein; 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.	0.629
Meso_0210	dnaQ	Meso_0210	Meso_3482	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	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.	0.638
Meso_0210	recA	Meso_0210	Meso_1263	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	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.	0.973
Meso_0210	ruvA	Meso_0210	Meso_3178	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	Holliday junction DNA helicase subunit RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.	0.710
Meso_0211	Meso_0210	Meso_0211	Meso_0210	Hypothetical protein.	Putative prophage repressor; PFAM: peptidase S24, S26A and S26B; KEGG: nar:Saro_3015 putative prophage repressor.	0.773
Meso_1582	Meso_0002	Meso_1582	Meso_0002	TIGRFAM: DNA polymerase III, delta prime subunit; KEGG: mlo:mll0423 DNA polymerase III, delta prime subunit.	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 [...]	0.998