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recD2 protein (Chlamydia trachomatis) - STRING interaction network
"recD2" - ATP-dependent RecD-like DNA helicase in Chlamydia trachomatis
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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
Others
textmining
co-expression
protein homology
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recD2ATP-dependent RecD-like DNA helicase; DNA-dependent ATPase and ATP-dependent 5’-3’ DNA helicase. Has no activity on blunt DNA or DNA with 3’-overhangs, requires at least 10 bases of 5’-ssDNA for helicase activity (746 aa)    
Predicted Functional Partners:
O172_03580
annotation not available (496 aa)
   
   
 
0.862
nrdA
Ribonucleoside-diphosphate reductase; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (1047 aa)
   
 
  0.764
recB
annotation not available (1026 aa)
 
 
  0.694
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (868 aa)
   
 
  0.694
topA
DNA topoisomerase 1; 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 [...] (857 aa)
   
 
  0.577
ytfF
annotation not available (341 aa)
   
        0.463
O172_03510
annotation not available (1006 aa)
   
 
  0.455
polC_1
annotation not available (232 aa)
 
   
  0.449
dnaN
Beta sliding clamp; 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 replication as [...] (366 aa)
   
 
  0.421
Your Current Organism:
Chlamydia trachomatis
NCBI taxonomy Id: 813
Other names: ATCC VR-571B, C. trachomatis, Chlamydia trachomatis, Chlamydozoon trachomatis, DSM 19440, Rickettsia trachomae, Rickettsia trachomatis, strain A/Har-13
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