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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ALX66154.1Hypothetical protein. (308 aa)    
Predicted Functional Partners:
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
   
 0.835
ALX66317.1
Hypothetical protein.
  
  0.796
ALX67150.1
Ubiquinol-cytochrome C reductase.
  
 
 0.758
ALX66155.1
Hypothetical protein.
 
     0.679
ALX66520.1
Ferredoxin.
   
 0.662
ALX67317.1
Succinate dehydrogenase; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
   
 
 0.634
ALX65617.1
Hypothetical protein.
  
   0.627
ALX65909.1
Hypothetical protein.
   
 
 0.588
ALX67153.1
Cytochrome C oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
    
 
 0.579
groL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
    
  0.503
Your Current Organism:
Microbacterium sp. XT11
NCBI taxonomy Id: 367477
Other names: M. sp. XT11
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.