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
OFA10260.1Outer membrane-specific lipoprotein transporter subunit LolE. (855 aa)    
Predicted Functional Partners:
macB_1
Macrolide export ATP-binding/permease protein MacB.
  
 
 0.951
OFA13142.1
Putative ABC transporter ATP-binding protein.
 
 
 0.945
guaA_1
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
 
  0.863
OFA10261.1
Hypothetical protein; Glutathione peroxidase homolog BsaA; Belongs to the glutathione peroxidase family.
       0.773
bceA
Bacitracin export ATP-binding protein BceA.
 
 
 0.563
nagZ
Beta-hexosaminidase precursor.
  
  
 0.546
dppE_8
Dipeptide-binding protein DppE precursor.
       0.530
copY
Transcriptional repressor CopY.
 
  
  0.528
secY
Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 
 0.488
lolD
Lipoprotein-releasing system ATP-binding protein LolD.
  
 
 0.479
Your Current Organism:
Lactobacillus sunkii
NCBI taxonomy Id: 481719
Other names: DSM 19904, JCM 15039, L. sunkii, Lactobacillus sp. YIT 11161, Lactobacillus sp. YIT 11442, Lactobacillus sp. YIT 11539, Lactobacillus sp. YIT 11549, Lactobacillus sp. YIT 11557, Lactobacillus sp. YIT 11635, Lactobacillus sunkii Watanabe et al. 2009, NRIC 0744, YIT 11161
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