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
ADO81989.1ATP synthase I; InterPro IPR008413; KEGG: fnu:FN0365 ATP synthase protein I, sodium ion specific; PFAM: ATP synthase I; SPTR: Q8KRV5 I-protein; PFAM: ATP synthase I chain. (127 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.
    
  0.967
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.
    
  0.954
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.
    
  0.936
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; Belongs to the ATPase delta chain family.
    
  0.936
atpA
ATP synthase F1 subcomplex 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.
    
  0.931
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.
    
  0.930
atpD
ATP synthase F1 subcomplex 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.
    
  0.925
atpC
ATP synthase F1 subcomplex epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
    
  0.925
ADO81988.1
Methyltransferase type 11; COGs: COG2226 Methylase involved in ubiquinone/menaquinone biosynthesis; InterPro IPR013216; KEGG: eel:EUBELI_00500 hypothetical protein; PFAM: Methyltransferase type 11; SPTR: C3WEX4 Putative uncharacterized protein; PFAM: Methyltransferase domain.
       0.430
Your Current Organism:
Ilyobacter polytropus
NCBI taxonomy Id: 572544
Other names: I. polytropus DSM 2926, Ilyobacter polytropus DSM 2926, Ilyobacter polytropus str. DSM 2926, Ilyobacter polytropus strain DSM 2926
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.