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
arnT4-amino-4-deoxy-L-arabinose lipid A transferase; 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. Belongs to the glycosyltransferase 83 family. (549 aa)    
Predicted Functional Partners:
arnD
4-deoxy-4-formamido-L-arabinose- phosphoundecaprenol deformylase; 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; Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.
 
 
 0.987
arnA
Bifunctional UDP-glucuronic acid oxidase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase; 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; In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily.
 
  
 0.973
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.
 
  
 0.964
arnF
4-amino-4-deoxy-L-arabinose-phospho-UDP flippase; Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane; Belongs to the ArnF family.
 
  
 0.934
arnE
4-amino-4-deoxy-L-arabinose-phospho-UDP flippase; Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane; Belongs to the ArnE family.
 
  
 0.923
ARQ74740.1
UDP-glucose 6-dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.830
ARQ74739.1
Glycosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.632
ARQ75373.1
Molecular chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.568
ARQ75369.1
Exotoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.554
B6D87_14640
Fimbrial protein; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.549
Your Current Organism:
Pseudomonas fragi
NCBI taxonomy Id: 296
Other names: ATCC 4973, Bacterium fragi, CCUG 556, CFBP 4556, CIP 55.4, DSM 3456, HAMBI 28, IFO 3458, LMG 2191, LMG:2191, NBRC 3458, NCCB 69033, NCIB 8542, NCIB:8542, NCTC 10689, NRRL B-25, NRRL B-727, NRRL:B:25, P. fragi, Pseudomonas fragariae, VKM B-898, VKM:B:898
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