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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
yebEannotation not available (219 aa)    
Predicted Functional Partners:
spy
An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins
   
  
 0.815
ldtC
L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp
   
  
 0.762
mdtA
Multidrug efflux pump membrane fusion protein mdta; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function
  
  
 0.649
yebF
annotation not available
  
 
 0.641
trxA
Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions
    
   0.637
yncJ
annotation not available
   
    0.550
yebG
Dna damage-inducible protein regulated by lexa; Uncharacterized protein YebG; Protein involved in DNA repair and SOS response
 
  
 0.549
dgcZ
Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules May act as a zinc sensor that controls, via c-di-GMP, post-translational events . Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...]
   
  
 0.509
ybgS
Putative periplasmic protein; Uncharacterized protein YbgS; Putative homeobox protein
  
     0.494
ptrB
Oligopeptidase b; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues
  
    0.482
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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