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
arnDPutative 4-deoxy-4-formamido-l-arabinose-phosphoundecaprenol deformylase arnd; Catalyzes the deformylation of 4-deoxy-4-formamido-L- arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose- phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (Probable) (296 aa)    
Predicted Functional Partners:
arnC
Undecaprenyl-phosphate 4-deoxy-4-formamido-l-arabinose transferase; Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides
 
 0.999
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
 
 0.999
arnA
UDP-4-amino-4-deoxy-L-arabinose formyltransferase / UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating); Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides
 
  
 0.997
arnF
Undecaprenyl-phosphate-alpha-L-Ara4N flippase - ArnF subunit; Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane
 
  
 0.995
arnE
Undecaprenyl-phosphate-alpha-L-Ara4N flippase - ArnE subunit; Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane
 
  
 0.994
arnB
Uridine 5'-(beta-1-threo-pentapyranosyl-4-ulose diphosphate) aminotransferase, plp-dependent; Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides
 
 
 0.990
ais
Putative lipopolysaccharide core heptose(ii)-phosphate phosphatase; Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core
  
  
 0.809
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
  
  
 0.724
yjaH
annotation not available
      
 0.640
yadE
Putative polysaccharide deacetylase lipoprotein; Uncharacterized protein YadE
      
 0.609
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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