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
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[Homology]
Score
palPart of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:11115123, PubMed:17233825). The Tol-Pal system is also required for polar localization of chemoreceptors clusters . (173 aa)    
Predicted Functional Partners:
tolB
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 . TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane . Is also involved in the uptake of some colicins A (PubMed:2687247, PubMed:7929011, PubMed:11994151). The Tol-Pal system is also required for polar localization of chemoreceptors clusters . ECO:0000269|PubMed:19696740, ECO:0000269|PubMed [...]
 
 0.999
ybgF
Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state.
 
 
 0.998
tolQ
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 . Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction . Is also involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA (PubMed:1683466, PubMed:3294803). The Tol-Pal system is also required for polar localization of chemoreceptors clusters . ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:24720726,
 
 
 0.996
tolR
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 . Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction .The Tol-Pal system is also required for polar localization of chemoreceptors clusters (PubMed:24720726, PubMed:11722743, PubMed:1683466, PubMed:17233825) (Probable). There are about 900 TolR molecules per cell . Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) [...]
 
 
 0.992
ompA
With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape . Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes . A very abundant protein, there can be up to 210,000 OmpA molecules per cell . Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at [...]
  
 
 0.992
ybgC
Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond.
     
 0.956
lpp
An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . The only protein known to be covalently linked to the peptidoglycan network (PGN) . Also non-covalently binds the PGN . The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (PubMed:4261992, PubMed:3013869, PubMed:4245367, PubMed:4565677). The most adundant cellular pr [...]
   
 
 0.944
lolA
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step
 
 
 0.939
bamA
Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there i [...]
  
 
 0.900
lolB
Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability
   
 
 0.884
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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