sbcD protein (Pseudomonas aeruginosa) - STRING interaction network

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sbcD

Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity (409 aa)

Predicted Functional Partners:

sbcC

0.999

DR97_4623

0.853

ORF54

0.853

recA

0.814

recD

0.807

DR97_5540

0.743

DR97_5371

0.743

DR97_1989

0.743

endA

0.732

recB

0.723

Your Current Organism:

Pseudomonas aeruginosa

NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
DR97_1989	recA	DR97_1989	DR97_4322	annotation not available	Protein RecA; 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	0.547
DR97_1989	sbcD	DR97_1989	DR97_1456	annotation not available	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.743
DR97_4623	sbcC	DR97_4623	DR97_1457	annotation not available	Nuclease sbcCD subunit C; recF/RecN/SMC N terminal domain protein	0.774
DR97_4623	sbcD	DR97_4623	DR97_1456	annotation not available	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.853
DR97_5371	recA	DR97_5371	DR97_4322	Conserved hypothetical protein	Protein RecA; 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	0.547
DR97_5371	sbcD	DR97_5371	DR97_1456	Conserved hypothetical protein	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.743
DR97_5540	recA	DR97_5540	DR97_4322	recF/RecN/SMC N terminal domain protein	Protein RecA; 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	0.547
DR97_5540	sbcD	DR97_5540	DR97_1456	recF/RecN/SMC N terminal domain protein	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.743
ORF54	sbcC	DR97_3749	DR97_1457	Uncharacterized protein	Nuclease sbcCD subunit C; recF/RecN/SMC N terminal domain protein	0.853
ORF54	sbcD	DR97_3749	DR97_1456	Uncharacterized protein	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.853
endA	recA	DR97_5209	DR97_4322	annotation not available	Protein RecA; 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	0.664
endA	sbcD	DR97_5209	DR97_1456	annotation not available	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.732
recA	DR97_1989	DR97_4322	DR97_1989	Protein RecA; 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	annotation not available	0.547
recA	DR97_5371	DR97_4322	DR97_5371	Protein RecA; 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	Conserved hypothetical protein	0.547
recA	DR97_5540	DR97_4322	DR97_5540	Protein RecA; 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	recF/RecN/SMC N terminal domain protein	0.547
recA	endA	DR97_4322	DR97_5209	Protein RecA; 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	annotation not available	0.664
recA	recB	DR97_4322	DR97_1459	Protein RecA; 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	RecBCD enzyme subunit RecB; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3’ direction. Cuts ssDNA a few nucleotides 3’ to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3’-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holo [...]	0.892
recA	recD	DR97_4322	DR97_1458	Protein RecA; 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	RecBCD enzyme subunit RecD; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3’ direction. Cuts ssDNA a few nucleotides 3’ to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3’-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holo [...]	0.883
recA	sbcC	DR97_4322	DR97_1457	Protein RecA; 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	Nuclease sbcCD subunit C; recF/RecN/SMC N terminal domain protein	0.624
recA	sbcD	DR97_4322	DR97_1456	Protein RecA; 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	Nuclease SbcCD subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity	0.814

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