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
ABI66492.1ATP synthase protein I, putative; A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex. (108 aa)    
Predicted Functional Partners:
atpB
ATP synthase F0 subcomplex A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
  
 
 0.906
atpE
ATP synthase F0 subcomplex 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.
 
 
 0.875
atpF1
H+-transporting two-sector ATPase, B/B' 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.
  
 
 0.836
atpF2
H+-transporting two-sector ATPase, B/B' 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.
 
 
 0.784
ABI64922.1
KEGG: bmb:BruAb2_0213 hypothetical protein.
  
     0.614
smc
Condensin subunit Smc; Required for chromosome condensation and partitioning. Belongs to the SMC family.
       0.592
atpH
ATP synthase F1 subcomplex 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.
  
 
 0.558
ABI66583.1
KEGG: rpc:RPC_0544 hypothetical protein.
  
     0.550
ABI64749.1
KEGG: rpb:RPB_0679 peptidoglycan-binding domain 1.
  
     0.527
ABI66488.1
KEGG: ccr:CC0376 hypothetical protein.
 
     0.521
Your Current Organism:
Maricaulis maris
NCBI taxonomy Id: 394221
Other names: M. maris MCS10, Maricaulis maris MCS10, Maricaulis maris str. MCS10, Maricaulis maris strain MCS10
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.