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
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; Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily. (297 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.
 
 
 0.996
arnA
Bifunctional polymyxin resistance protein ArnA; 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.
 
  
 0.987
arnT_3
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl 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.
 
  
 0.981
arnE
Putative 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE; 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.
 
  
 0.980
arnF
Putative 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF; 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.
 
  
 0.950
arnT_1
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase.
 
  
 0.923
arnB
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate 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.
 
  
 0.893
wbbD_2
UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-galactosyltransferase.
  
  
 0.704
arnT_2
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase.
 
  
 0.644
mepS_1
Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase precursor.
     
 0.560
Your Current Organism:
Providencia rettgeri
NCBI taxonomy Id: 587
Other names: ATCC 29944, Bacterium rettgeri, CCUG 14804, CIP 103182, DSM 4542, LMG 3259, LMG:3259, NCTC 11801, P. rettgeri, Proteus rettgeri, Shigella rettgeri
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