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
EU95_0807Scaffold protein for 4Fe-4S cluster assembly; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (356 aa)    
Predicted Functional Partners:
EU95_0540
Polysaccharide export-related periplasmic protein; Alternative locus ID: PMIT9201_0505.
  
 0.879
EU95_0809
Signal transduction histidine kinase; Alternative locus ID: PMIT9201_0632.
     
 0.838
rodA
Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily.
       0.825
ndhI
NAD(P)H-quinone oxidoreductase chain I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family.
    
 0.819
ndhJ
NAD(P)H-quinone oxidoreductase chain J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
     
 0.812
ndhH
NAD(P)H-quinone oxidoreductase chain H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
     
 0.812
EU95_1091
Hypothetical protein; Alternative locus ID: PMIT9201_1128; COG1565: Uncharacterized conserved protein.
     
 0.789
ndhK
NAD(P)H-quinone oxidoreductase chain K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family.
     
 0.789
EU95_0625
Putative chaperon-like protein Ycf39 for quinone binding in Photosystem II; Alternative locus ID: PMIT9201_0590.
   
 
  0.651
EU95_1189
Hypothetical protein; Alternative locus ID: PMIT9201_1226.
   
 
  0.651
Your Current Organism:
Prochlorococcus marinus MIT9201
NCBI taxonomy Id: 93057
Other names: P. marinus str. MIT 9201, Prochlorococcus marinus str. MIT 9201, Prochlorococcus sp. MIT 9201, Prochlorococcus sp. MIT9201
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