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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
bcsBCyclic di-GMP-binding protein precursor; Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP); Belongs to the AcsB/BcsB family. (751 aa)    
Predicted Functional Partners:
bcsA
Cellulose synthase catalytic subunit; Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose.
 
 0.999
bcsZ
Endoglucanase precursor.
 
  
 0.982
Lche_1037
Hypothetical protein.
 
 
 
 0.971
bcsC
Cellulose synthase operon protein C precursor.
 
 
 0.830
parA
Chromosome partitioning protein ParA.
  
 
 0.688
Lche_0801
Hypothetical protein.
   
 
 0.665
htpG
Class III heat-shock protein HtpG(molecular chaperone); Molecular chaperone. Has ATPase activity.
   
 0.563
yjeA
Endo-1,4-beta-xylanase.
   
 0.558
pagP
Antimicrobial peptide resistance and Lipid A acylation protein PagP; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
  
     0.547
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.519
Your Current Organism:
Legionella cherrii
NCBI taxonomy Id: 28084
Other names: ATCC 35252, CCUG 29666, CIP 103842, DSM 19213, L. cherrii, Legionella cherryi, NCTC 11976, strain ORW
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