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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
atpCF0F1-type ATP synthase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa)    
Predicted Functional Partners:
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.
 
 0.997
atpD
F-type H+-transporting ATPase beta chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.
 
 0.995
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. Belongs to the ATPase alpha/beta chains family.
 
 0.995
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; Belongs to the ATPase delta chain family.
 
 0.995
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.
 
 0.994
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.
 
 0.993
atpB
F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
 
 0.993
atpG-2
F0F1 ATP 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.
 
 0.984
atpA-2
F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
 
 0.981
atpD-2
F0F1 ATP 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; Belongs to the ATPase alpha/beta chains family.
 
 0.980
Your Current Organism:
Roseburia hominis
NCBI taxonomy Id: 585394
Other names: R. hominis A2-183, Roseburia hominis A2-183, Roseburia hominis str. A2-183, Roseburia hominis strain A2-183, butyrate-producing bacterium A2-183
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