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
atpDATP 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; Belongs to the ATPase alpha/beta chains family. (461 aa)    
Predicted Functional Partners:
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.
 
 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
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.
 
 0.999
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; Belongs to the ATPase delta chain family.
 
 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. Belongs to the ATPase alpha/beta chains family.
 
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
atpC
ATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
 0.999
ADH61913.1
PFAM: H+transporting two-sector ATPase C subunit; KEGG: tpd:Teth39_2263 V-type ATP synthase subunit K.
  
 0.991
ADH60604.1
KEGG: tpd:Teth39_1457 NADH dehydrogenase (quinone); PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; Sucraseferredoxin family protein; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; 4Fe-4S ferredoxin iron-sulfur binding domain protein.
  
 0.954
ADH61650.1
TIGRFAM: translation elongation factor G; small GTP-binding protein; PFAM: protein synthesis factor GTP-binding; elongation factor G domain protein; elongation factor G domain IV; elongation factor Tu domain 2 protein; KEGG: tpd:Teth39_0336 elongation factor G; SMART: elongation factor G domain IV; elongation factor G domain protein.
  
 
 0.938
Your Current Organism:
Thermoanaerobacter mathranii
NCBI taxonomy Id: 583358
Other names: T. mathranii subsp. mathranii str. A3, Thermoanaerobacter mathranii subsp. mathranii A3, Thermoanaerobacter mathranii subsp. mathranii DSM 11426, Thermoanaerobacter mathranii subsp. mathranii str. A3, Thermoanaerobacter mathranii subsp. mathranii strain A3
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.