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rho protein (Sideroxydans lithotrophicus) - STRING interaction network
"rho" - Transcription termination factor Rho in Sideroxydans lithotrophicus
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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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Score
rhoTranscription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho’s RNA-dependent ATPase activity, and release of the mRNA from the DNA template (418 aa)    
Predicted Functional Partners:
nusG
NusG antitermination factor; Participates in transcription elongation, termination and antitermination (177 aa)
     
 
  0.907
hfq
RNA chaperone Hfq; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs (76 aa)
     
 
  0.899
Slit_2060
Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (568 aa)
 
   
  0.766
Slit_2833
DNA polymerase I (929 aa)
   
   
  0.754
Slit_1011
Thioredoxin (108 aa)
   
   
  0.748
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (354 aa)
   
   
  0.682
rpoH
RNA polymerase, sigma 32 subunit, RpoH (289 aa)
   
 
  0.656
secY
Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (435 aa)
 
   
  0.640
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1356 aa)
   
 
  0.612
tig
Trigger factor; 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 (434 aa)
   
 
  0.604
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus, S. lithotrophicus ES-1, Siderooxidans, Siderooxidans lithoautotrophicus, Sideroxydans, Sideroxydans lithotrophicus, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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