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
KXB80278.1ATP synthase, delta/epsilon subunit, beta-sandwich domain protein; KEGG: pdn:HMPREF9137_1013 1.3e-23 ATP synthase subunit delta/epsilon; K02114 F-type H+-transporting ATPase subunit epsilon; Psort location: Cytoplasmic, score: 8.96. (79 aa)    
Predicted Functional Partners:
atpD
ATP synthase F1, beta subunit; 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
atpB
ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
  
 0.999
atpE
ATP synthase F0, C subunit; 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.
  
 0.999
atpH
ATP synthase F1, delta subunit; 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.
  
 0.999
atpA
ATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
  
 0.999
atpG
ATP synthase F1, gamma subunit; 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.
  
 0.999
atpF
ATP synthase F0, B subunit; 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
KXB80430.1
WbqC-like protein; KEGG: fna:OOM_0806 3.8e-08 cysteine dioxygenase; Psort location: Cytoplasmic, score: 8.96.
  
 0.994
KXB78018.1
Respiratory-chain NADH dehydrogenase, subunit; KEGG: pdn:HMPREF9137_1116 8.1e-246 hypothetical protein; K13378 NADH-quinone oxidoreductase subunit C/D; Psort location: Cytoplasmic, score: 9.12.
  
 
 0.994
rplL
Ribosomal protein L7/L12; 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.
   
  
 0.829
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 419005
Other names: CCUG 53648, DSM 23384, JCM 14753, P. amnii, Prevotella amnii Lawson et al. 2008 emend. Hahnke et al. 2016
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.