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priA protein (Ruminococcus sp. 5139BFAA) - STRING interaction network
"priA" - ATP-dependent helicase PriA in Ruminococcus sp. 5139BFAA
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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priAATP-dependent helicase PriA ; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA (739 aa)    
Predicted Functional Partners:
RSAG_03249
Replicative DNA helicase ; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity (442 aa)
   
  0.956
RSAG_03244
Single-stranded DNA-binding protein (153 aa)
       
 
  0.872
RSAG_02370
UDP-N-acetylmuramyl-tripeptide synthetase (491 aa)
              0.859
RSAG_02375
Ribosomal RNA small subunit methyltransferase B (450 aa)
 
        0.788
fmt
Methionyl-tRNA formyltransferase ; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (324 aa)
   
   
  0.767
RSAG_00520
Single-stranded-DNA-specific exonuclease RecJ (570 aa)
 
   
  0.757
recR
Recombination protein RecR ; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO (199 aa)
   
 
  0.751
RSAG_02379
Ribosome small subunit-dependent GTPase A ; May play a role in 30S ribosomal subunit biogenesis. Unusual circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover (292 aa)
   
   
  0.737
RSAG_02380
Ribulose-phosphate 3-epimerase (223 aa)
     
      0.733
def
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (158 aa)
   
   
  0.728
Your Current Organism:
Ruminococcus sp. 5139BFAA
NCBI taxonomy Id: 457412
Other names: R. sp. 5_1_39BFAA, Ruminococcus 5_1_39BFAA, Ruminococcus sp. 5139BFAA, Ruminococcus sp. 5_1_39BFAA
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