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recA protein (Dehalogenimonas lykanthroporepellens) - STRING interaction network
"recA" - Recombinase A in Dehalogenimonas lykanthroporepellens
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query proteins and first shell of interactors
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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
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textmining
co-expression
protein homology
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recARecombinase 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 (342 aa)    
Predicted Functional Partners:
Dehly_0095
DNA polymerase I (915 aa)
   
  0.994
Dehly_0426
DNA-directed DNA polymerase (393 aa)
   
  0.994
Dehly_0318
RecQ family ATP-dependent DNA helicase (690 aa)
     
  0.990
Dehly_0949
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)
   
  0.985
recX
Regulatory protein RecX; Modulates RecA activity (185 aa)
   
 
  0.985
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 (412 aa)
   
  0.980
Dehly_1187
DNA polymerase III subunit beta (419 aa)
   
  0.980
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 [...] (698 aa)
   
  0.977
sbcC
SMC domain-containing protein; 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 (863 aa)
   
  0.963
mutL
DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (562 aa)
   
  0.956
Your Current Organism:
Dehalogenimonas lykanthroporepellens
NCBI taxonomy Id: 552811
Other names: Chloroflexi bacterium BL-DC-8, Chloroflexi bacterium BL-DC-9, D. lykanthroporepellens, D. lykanthroporepellens BL-DC-9, Dehalogenimonas, Dehalogenimonas lykanthroporepellens, Dehalogenimonas lykanthroporepellens BL-DC-9, Dehalogenimonas lykanthroporepellens str. BL-DC-9, Dehalogenimonas lykanthroporepellens strain BL-DC-9
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