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
HY22_02465ATP synthase subunit epsilon; Derived by automated computational analysis using gene prediction method: Protein Homology. (90 aa)    
Predicted Functional Partners:
atpD
ATP F0F1 synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
  
 0.999
atpA
ATP F0F1 synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
  
 0.998
atpG
ATP F0F1 synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
  
 0.998
atpH
Hypothetical protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
 
 0.998
atpF
ATP F0F1 synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
  
 0.998
atpE
Hypothetical protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
  
 0.998
HY22_09905
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.879
rplL
Hypothetical protein; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
   
  
 0.868
rplQ
50S ribosomal protein L17; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.867
nuoB
NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
 
 0.823
Your Current Organism:
Thermochlorobacteriaceae bacterium GBChlB
NCBI taxonomy Id: 1519464
Other names: C. Thermochlorobacteriaceae bacterium GBChlB, Candidatus Thermochlorobacteriaceae bacterium GBChlB, Chlorobium sp. GBChlB
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.