STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
priAPrimosomal protein N' (replication factor Y); 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; Belongs to the helicase family. PriA subfamily. (691 aa)    
Predicted Functional Partners:
Krad_2990
Phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family.
  
    0.924
rpoZ
DNA-directed RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
 
     0.883
Krad_4338
TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; nucleic acid binding OB-fold tRNA/helicase-type; KEGG: aau:AAur_4164 single-strand binding protein.
 
 
 
 0.866
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
    0.843
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
       0.828
whiA
Protein of unknown function DUF199; Involved in cell division and chromosome segregation.
 
     0.797
Krad_2992
Guanylate kinase; Essential for recycling GMP and indirectly, cGMP.
  
    0.761
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: art:Arth_1490 phenylalanyl-tRNA synthetase, beta subunit.
 
  
 0.713
Krad_4333
Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily.
   
 0.697
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
  
  
 0.681
Your Current Organism:
Kineococcus radiotolerans
NCBI taxonomy Id: 266940
Other names: K. radiotolerans SRS30216 = ATCC BAA-149, Kineococcus radiotolerans ATCC BAA-149, Kineococcus radiotolerans ATCC BAA-149 = SRS30216, Kineococcus radiotolerans SRS30216, Kineococcus radiotolerans SRS30216 = ATCC BAA-149, Kineococcus-like str. SRS30216
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.