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
RP802ATP SYNTHASE GAMMA CHAIN (atpG); 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. (288 aa)    
Predicted Functional Partners:
RP022
ATP SYNTHASE C CHAIN (atpE); 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
RP023
ATP SYNTHASE A CHAIN (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
 
 0.999
RP800
ATP SYNTHASE EPSILON CHAIN (atpC); Produces ATP from ADP in the presence of a proton gradient across the membrane.
  
 0.999
RP801
ATP SYNTHASE BETA CHAIN (atpD); 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
RP803
ATP SYNTHASE ALPHA CHAIN (atpA); 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
RP804
ATP SYNTHASE DELTA CHAIN (atpH); 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
RP020
ATP SYNTHASE B CHAIN PRECURSOR (atpF); 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.
  
 0.996
RP021
ATP SYNTHASE B CHAIN (atpX).
  
 0.996
RP653
30S RIBOSOMAL PROTEIN S3 (rpsC); 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.
  
 
 0.969
RP272
CYTOCHROME C1, HEME PROTEIN PRECURSOR (fbcH).
   
 
 0.964
Your Current Organism:
Rickettsia prowazekii
NCBI taxonomy Id: 272947
Other names: R. prowazekii str. Madrid E, Rickettsia prowazekii str. Madrid E, Rickettsia prowazekii strain Madrid E
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