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
waaCheptsyl_trn_I: lipopolysaccharide heptosyltransferase I. (326 aa)    
Predicted Functional Partners:
waaF
heptsyl_trn_II: lipopolysaccharide heptosyltransferase II.
 
 0.991
LO55_2106
Glycosyl transferases group 1 family protein; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family.
 
  
 0.966
LO55_1435
4Fe-4S dicluster domain protein.
  
   0.944
LO55_1645
Glycosyltransferase 9 family protein.
 
 
 0.926
LO55_2973
NDH_I_M: proton-translocating NADH-quinone oxidoreductase, chain M family protein.
    
 
 0.891
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain N family protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family.
    
 
 0.887
nuoH
NADH dehydrogenase family protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
   
   0.872
nuoB
NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
    
 
 0.870
rfaE1-2
rfaE_dom_I: bifunctional protein RfaE, domain I.
 
  
 0.865
nuoD
NADH dehydrogenase (quinone), D subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
    
 
 0.862
Your Current Organism:
Massilia timonae
NCBI taxonomy Id: 47229
Other names: CCUG 45783, CIP 105350, Janthinobacterium sp. R2-11, M. timonae, Massilia timonae La Scola et al. 2000 emend. Lindquist et al. 2003, Timone isolate, strain UR/MT95
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