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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
arnDPolysaccharide deacetylase; 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. (298 aa)    
Predicted Functional Partners:
arnC
Glycosyl transferase, family 2; 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.
 
 
 0.996
arnT
Glycosyl transferase, family 39; 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.
 
 
 0.989
arnA
NAD-dependent epimerase/dehydratase; 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 C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
 
  
 0.972
arnE
Small multidrug resistance protein; 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.
 
  
 0.965
arnF
Conserved hypothetical protein; 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.
 
  
 0.914
arnB
DegT/DnrJ/EryC1/StrS aminotransferase; 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; Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
 
  
 0.911
ABP62585.1
Cellulose synthase (UDP-forming); Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose.
  
  
 0.616
ABP62595.1
Cellulose synthase (UDP-forming); Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose.
  
  
 0.616
ABP59624.1
PFAM: Haemolysin expression modulating family protein; KEGG: stm:STM0473 hemolysin expression modulating protein (involved in environmental regulation of virulence factors).
  
     0.463
Your Current Organism:
Enterobacter sp. 638
NCBI taxonomy Id: 399742
Other names: E. sp. 638
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.