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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
atpGH(+)-transporting two-sector ATPase; 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. (286 aa)    
Predicted Functional Partners:
atpC
F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
 0.999
atpD
F0F1 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; Belongs to the ATPase alpha/beta chains family.
 0.999
atpA
H(+)-transporting two-sector ATPase; 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
H(+)-transporting two-sector ATPase; 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
F0F1 ATP synthase subunit B; 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
atpE
F0F1 ATP synthase subunit C; 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
atpB
F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
 
 0.999
rpsC
Ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
  
 
 0.967
rpsK
30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
   
 
 0.954
Tgr7_0751
PFAM: cytochrome c1; KEGG: vfi:VF_2217 cytochrome c1.
   
 
 0.953
Your Current Organism:
Thioalkalivibrio sulfidiphilus
NCBI taxonomy Id: 396588
Other names: T. sulfidiphilus HL-EbGr7, Thioalkalivibrio sp. HL-EbGR7, Thioalkalivibrio sulfidiphilus HL-EbGr7, Thioalkalivibrio sulfidiphilus str. HL-EbGr7, Thioalkalivibrio sulfidiphilus strain HL-EbGr7, Thioalkalivibrio sulfidophilus HL-EbGr7
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.