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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
sigA,Putative principal RNA polymerase sigma factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. (396 aa)    
Predicted Functional Partners:
dnaG
CHC2 zinc finger:Toprim domain; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
  
 0.869
rpoA
Bacterial RNA polymerase, alpha chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.802
rpoB
RNA polymerase beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.784
priA
Primosomal 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.
 
    0.641
rpoZ
Putative DNA-directed RNA polymerase (omega chain); 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.
   
 
 0.610
rpoC2
RNA polymerase beta prime subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
   
 
 0.605
hemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
  
    0.581
nusG
Transcription antitermination protein, NusG; Participates in transcription elongation, termination and antitermination.
   
  
 0.549
lrtA
Light repressed protein A homolog; Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.
   
  
 0.519
trmD
Putative bifuntional enzyme: tRNA methyltransferase; Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP); Belongs to the RNA methyltransferase TrmD family.
 
    0.517
Your Current Organism:
Prochlorococcus marinus pastoris
NCBI taxonomy Id: 59919
Other names: P. marinus subsp. pastoris str. CCMP1986, Prochlorococcus marinus MED4, Prochlorococcus marinus subsp. pastoris str. CCMP1378, Prochlorococcus marinus subsp. pastoris str. CCMP1986, Prochlorococcus sp. CCMP1378, Prochlorococcus sp. MED4
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