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
ldtCL,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. (320 aa)    
Predicted Functional Partners:
spy
Periplasmic ATP-independent protein refolding chaperone, stress-induced; 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 prote [...]
  
  
 0.986
yebE
DUF533 family inner membrane protein.
   
  
 0.984
mdtA
Multidrug efflux system, subunit A; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
  
  
 0.981
ldtD
Murein L,D-transpeptidase; Responsible, at least in part, for generating a meso- diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link. Belongs to the YkuD family.
 
  
 0.947
mdtB
Multidrug efflux system, subunit B; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.
   
    0.873
chaA
Calcium/sodium:proton antiporter; Sodium exporter that functions mainly at alkaline pH. Can also function as a potassium/proton and calcium/proton antiporter at alkaline pH. Does not play a major role in calcium export.
   
  
 0.806
yafK
L,D-transpeptidase-related protein.
 
  
 0.796
mdtC
Multidrug efflux system, subunit C; The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.
   
    0.792
acrD
Aminoglycoside/multidrug efflux system; Participates in the efflux of aminoglycosides. Confers resistance to a variety of these substances. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
   
  
 0.745
baeS
Sensory histidine kinase in two-component regulatory system with BaeR; Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress. Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression. Activates BaeR by phosphorylation which then activates the mdtABCD and probably the CRISPR-Cas casABCDE-ygbT-ygbF operons.
  
    0.708
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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
Server load: medium (56%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.