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
pmrDInactive two-component system connector protein; Interacts with phosphorylated BasR protein to mediate transcriptional induction of BasR-activated genes to induce polymyxin resistance in some natural isolates (88 aa)    
Predicted Functional Partners:
basR
Response regulator in two-component regulatory system with bass; Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin (By similarity)
   
 
 0.995
basS
Sensory histidine kinase in two-component regulatory system with basr; Member of the two-component regulatory system BasS/BasR Autophosphorylates and activates BasR by phosphorylation
      
 0.956
phoP
Response regulator in two-component regulatory system with phoq; Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). Mediates magnesium influx to the cytosol by activation of MgtA. Pro [...]
   
  
 0.911
phoQ
Sensory histidine kinase in two-component regulatory system with phop; Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP- repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulti [...]
   
  
 0.890
eptA
Lipid a ethanolaminephosphotransferase; Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin
      
 0.878
ugd
Udpglucose 6-dehydrogenase; UDP-glucose 6-dehydrogenase; Protein involved in cell surface antigen activity, host-interacting, colanic acid biosynthetic process and response to desiccation
      
 0.874
mgrB
Regulatory peptide for phopq, feedback inhibition; Represses PhoP/PhoQ signaling, possibly by binding to the periplasmic domain of PhoQ, altering its activity and that of downstream effector PhoP. PhoP-regulated transcription is redox- sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, and thus PhoP
   
  
 0.849
lpxT
Kdo2-lipid A phosphotransferase; Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1- diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P) . In vitro, has low undecaprenyl-diphosphate phosphatase activity
      
 0.790
ais
Putative lipopolysaccharide core heptose(ii)-phosphate phosphatase; Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core
      
 0.790
arnT
Lipid iva 4-amino-4-deoxy-l-arabinosyltransferase; Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides
      
 0.790
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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