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
mppMpp; Mitochondrial processing protease; psort: bacterial cytoplasm --- Certainty= 0.244(Affirmative); COG0612 PqqL predicted Zn-dependent peptidases; Belongs to the peptidase M16 family. (436 aa)    
Predicted Functional Partners:
petC
Cytochrome c1, heme protein precursor; Psort: bacterial inner membrane --- Certainty= 0.317(Affirmative); COG2857 CYT1 cytochrome c1.
   
 0.986
petB
Cytochrome B (petB); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
    
  0.959
petA
Cytochrome B6-F complex iron-sulfur subunit (petA); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
   
  0.932
petA-2
Cytochrome B6-F complex iron-sulfur subunit (petA); Psort: bacterial cytoplasm --- Certainty= 0.295(Affirmative); split domain; COG0723 QcrA Rieske Fe-S protein.
   
  0.932
nuoF
NADH dehydrogenase I chain F (nuoF); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
   0.924
nuoI
NADH dehydrogenase I chain I (nuoI); 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.
  
   0.922
nuoG
NADH dehydrogenase I chain G (nuoG); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.
   
 
 0.921
nuoE
NADH dehydrogenase I chain E (nuoE); Psort: bacterial cytoplasm --- Certainty= 0.446(Affirmative); COG1905 NuoE NADH:ubiquinone oxidoreductase 24 kD subunit.
   
   0.900
AMF_1013
NADH-ubiquinone oxidoreductase, putative; Psort: bacterial inner membrane --- Certainty= 0.102(Affirmative); COG0702 Predicted nucleoside-diphosphate-sugar epimerases.
   
 
 0.870
nuoD
NADH dehydrogenase chain D (nuoD); 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.
   
   0.857
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
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