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
atpFATP 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. (186 aa)    
Predicted Functional Partners:
atpB
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.
 
 0.999
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
atpA
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
atpG
ATP 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.
 
 0.999
atpD
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
Arch_0368
ATPase, F1 complex, delta/epsilon subunit; COGs: COG0355 F0F1-type ATP synthase epsilon subunit (mitochondrial delta subunit); InterPro IPR020546; KEGG: bcv:Bcav_1308 H+transporting two-sector ATPase delta/epsilon subunit; PFAM: ATPase, F1 complex, delta/epsilon subunit-like; SPTR: C5C1U9 H+transporting two-sector ATPase delta/epsilon subunit; PFAM: ATP synthase, Delta/Epsilon chain, beta-sandwich domain.
 
 0.999
ppa
Inorganic diphosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
   
 
 0.950
tsf
Translation elongation factor Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family.
  
  
 0.904
rpsL
Ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
   
  
 0.901
Your Current Organism:
Arcanobacterium haemolyticum
NCBI taxonomy Id: 644284
Other names: A. haemolyticum DSM 20595, Arcanobacterium haemolyticum ATCC 9345, Arcanobacterium haemolyticum CIP 103370, Arcanobacterium haemolyticum DSM 20595, Arcanobacterium haemolyticum str. DSM 20595, Arcanobacterium haemolyticum strain DSM 20595
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