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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Cooccurrence
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[Homology]
Score
atpAPROBABLE ATP SYNTHASE ALPHA CHAIN PROTEIN; 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. (547 aa)    
Predicted Functional Partners:
atpB
ATP SYNTHASE F0 SUBUNIT 6; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
 
 0.999
atpE
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
atpF
ATP synthase B 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
atpH
H+-ATPASE 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
atpG
ATP SYNTHASE 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 ALPHA 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
atpC
PROBABLE ATP SYNTHASE EPSILON CHAIN PROTEIN; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
 0.999
odhA
2-OXOGLUTARATE DEHYDROGENASE; Catalyzes the E1 and E2 reactions as part of 2-oxoglutarate dehydrogenase (ODH) activity, to convert 2-oxoglutarate to succinyl-CoA and CO(2). OdhA has reductase activity with 2-oxoglutarate but does not react with pyruvate, and also displays transsuccinylase but no transacetylase activity. Since OdhA is not lipoylated, the succinyltransferase activity of its E2 domain is dependent on lipoyl residues of the acetyltransferase AceF.
  
 
 0.983
rpoB
DNA-DIRECTED RNA POLYMERASE BETA CHAIN; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 
  
 0.968
fusA
ELONGATION FACTOR G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
   
 
 0.966
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
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