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
atpAATP synthase alpha chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (503 aa)    
Predicted Functional Partners:
atpB
ATP synthase 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.
 
0.999
atpE
ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
 0.999
atpC
ATP synthase gamma chain; 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 delta chain; 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 B chain; 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
atpG
ATP synthase B' chain; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. Belongs to the ATPase B chain family.
 0.999
atpH
ATP synthase C chain; 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
atpI
ATP synthase A chain; 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
hoxF
NAD-reducing hydrogenase subunit HoxF; Sly1009910.
   
 
 0.989
ndhH
NAD(P)H-quinone oxidoreductase chain H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
 
 
 0.962
Your Current Organism:
Synechocystis sp. PCC6714
NCBI taxonomy Id: 1147
Other names: Aphanocapsa sp. (strain 5.3A), Aphanocapsa sp. 5-3A, Aphanocapsa sp. 5.3A, S. sp. PCC 6714, Synechocystis sp. (ATCC 27178), Synechocystis sp. (PCC 6714), Synechocystis sp. (strain PCC 6714), Synechocystis sp. ATCC 27178, Synechocystis sp. PCC 6714, Synechocystis sp. SAG 92.79, Synechocystis sp. UTCC 98, Synechocystis sp. UTEX 2470
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