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
BAB1_1985Unnamed protein product. (886 aa)    
Predicted Functional Partners:
tolB
TolB, N-terminal; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
  
 
 0.863
BAB1_1575
RNA-binding region RNP-1 (RNA recognition motif):Blue (type 1) copper domain.
  
    0.776
BAB1_1576
Conserved hypothetical protein.
  
     0.775
BAB1_1574
Protein of unknown function DUF58.
  
     0.773
BAB1_1186
Conserved hypothetical protein.
  
     0.766
BAB1_1760
TPR repeat.
  
   
 0.726
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
 
  0.698
BAB1_0898
Glycoside hydrolase, family 3, N-terminal.
  
  
 0.674
BAB1_1884
Conserved hypothetical protein.
  
    0.669
secY
C-5 cytosine-specific DNA methylase:SecY protein; 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.
   
 
 0.654
Your Current Organism:
Brucella abortus
NCBI taxonomy Id: 359391
Other names: B. abortus 2308, Brucella abortus 2308, Brucella melitensis biovar Abortus 2308
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.