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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
nusATranscription elongation factor NusA; Modifies transcription through interactions with RNA polymerase affecting elongation, readthrough, termination, and antitermination; Derived by automated computational analysis using gene prediction method: Protein Homology. (495 aa)    
Predicted Functional Partners:
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; beta subunit is part of the catalytic core which binds with a sigma factor to produce the holoenzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.997
KOH19469.1
DNA-directed RNA polymerase subunit alpha; Catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Dimerization of the alpha subunit is the first step in the sequential assembly of subunits to form the holoenzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.997
nusG
Transcription antiterminator NusG; Participates in transcription elongation, termination and antitermination.
 
 
 0.994
InfB
Translation initiation factor IF-2; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.991
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
   0.990
rpsB
30S ribosomal protein S2; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS2 family.
 
 
 0.984
rpsJ
30S ribosomal protein S10; NusE; involved in assembly of the 30S subunit; in the ribosome, this protein is involved in the binding of tRNA; in Escherichia coli this protein was also found to be involved in transcription antitermination; NusB/S10 heterodimers bind boxA sequences in the leader RNA of rrn operons which is required for antitermination; binding of NusB/S10 to boxA nucleates assembly of the antitermination complex; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.983
rimP
Ribosome maturation protein RimP; Required for maturation of 30S ribosomal subunits. Belongs to the RimP family.
  
  
 0.982
KOH19468.1
30S ribosomal protein S4; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.977
rplA
50S ribosomal protein L1; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uL1 family.
  
 
 0.974
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.