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
atpGATP 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. (295 aa)    
Predicted Functional Partners:
atpC
ATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
 0.999
atpD-2
ATP 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.
 0.999
atpA-2
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
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
atpF-2
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
atpB-2
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.
  
 0.997
Smon_0252
PFAM: H+transporting two-sector ATPase C subunit; KEGG: GH22892 gene product from transcript GH22892- RA; Belongs to the V-ATPase proteolipid subunit family.
  
 0.933
Smon_1215
TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: pyridine nucleotide-disulphide oxidoreductase dimerisation region; FAD-dependent pyridine nucleotide- disulphide oxidoreductase; glucose-inhibited division protein A; biotin/lipoyl attachment domain-containing protein; KEGG: gdi:GDI1418 2-oxoglutarate dehydrogenase E3 component.
  
 
 0.922
Smon_0532
Inorganic diphosphatase; PFAM: DHHA2 domain protein; phosphoesterase RecJ domain protein; KEGG: bca:BCE_2854 putative manganese-dependent inorganic pyrophosphatase.
     
 0.909
Your Current Organism:
Streptobacillus moniliformis
NCBI taxonomy Id: 519441
Other names: S. moniliformis DSM 12112, Streptobacillus moniliformis ATCC 14647, Streptobacillus moniliformis DSM 12112, Streptobacillus moniliformis str. DSM 12112, Streptobacillus moniliformis strain DSM 12112
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