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
EHQ02498.1ATPase, F1 complex, delta/epsilon subunit; PFAM: ATP synthase, Delta/Epsilon chain, beta-sandwich domain; COGs: COG0355 F0F1-type ATP synthase epsilon subunit (mitochondrial delta subunit); InterPro IPR020546; KEGG: zpr:ZPR_4514 ATP synthase subunit epsilon; PFAM: ATPase, F1 complex, delta/epsilon subunit, N-terminal; SPTR: ATP synthase subunit epsilon. (93 aa)    
Predicted Functional Partners:
atpB
ATP synthase F0 subcomplex 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 subcomplex 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 subcomplex 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 subcomplex 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 subunit alpha; 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 subcomplex 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
atpD
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.
 
 0.998
EHQ02501.1
PFAM: ATP synthase alpha/beta family, beta-barrel domain; ATP synthase alpha/beta family, nucleotide-binding domain; TIGRFAM: ATP synthase, F1 beta subunit; COGs: COG0055 F0F1-type ATP synthase beta subunit; InterPro IPR003593:IPR004100:IPR000194:IPR005722; KEGG: gfo:GFO_3548 F0F1 ATP synthase subunit beta; PFAM: ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain; ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal; SMART: ATPase, AAA+ type, core; SPTR: ATP synthase subunit beta; TIGRFAM: ATPase, F1 complex, beta subunit; manually curated.
 
 0.993
EHQ01289.1
InterPro IPR001450; KEGG: kdi:Krodi_2456 4Fe-4S ferredoxin, iron-sulfur binding-protein; PFAM: 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; SPTR: 4Fe-4S ferredoxin, iron-sulfur binding-protein.
  
 
 0.869
ppa
Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
   
 
  0.864
Your Current Organism:
Gillisia limnaea
NCBI taxonomy Id: 865937
Other names: G. limnaea DSM 15749, Gillisia limnaea DSM 15749, Gillisia limnaea R-8282, Gillisia limnaea str. DSM 15749, Gillisia limnaea strain DSM 15749
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.