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recD protein (Pseudonocardia dioxanivorans) - STRING interaction network
"recD" - Exodeoxyribonuclease V subunit alpha in Pseudonocardia dioxanivorans
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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recDExodeoxyribonuclease V subunit alpha; 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 re [...] (721 aa)    
Predicted Functional Partners:
recB
Exodeoxyribonuclease V subunit beta; 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 rep [...] (1137 aa)
 
  0.998
recC
Exodeoxyribonuclease V subunit gamma; 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 re [...] (1124 aa)
 
  0.998
tig
Trigger factor Tig; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (494 aa)
 
 
 
  0.749
Psed_0002
DNA polymerase III subunit beta; 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 beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA (376 aa)
   
 
  0.739
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (952 aa)
   
 
  0.706
Psed_6553
Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] (395 aa)
 
 
 
  0.677
recA
Recombinase A; 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 (347 aa)
   
 
  0.676
Psed_6547
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE (871 aa)
         
  0.653
Psed_3481
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE (875 aa)
         
  0.653
Psed_2213
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE (874 aa)
         
  0.653
Your Current Organism:
Pseudonocardia dioxanivorans
NCBI taxonomy Id: 675635
Other names: Actinobispora, Amycolata, P. dioxanivorans, P. dioxanivorans CB1190, Pseudamycolata, Pseudoamycolata, Pseudonocardia, Pseudonocardia dioxanivorans, Pseudonocardia dioxanivorans CB1190, Pseudonocardia dioxanivorans DSM 44775, Pseudonocardia dioxanivorans Mahendra and Alvarez-Cohen 2005, Pseudonocardia dioxanivorans str. CB1190, Pseudonocardia dioxanivorans strain CB1190
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