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
pbgP3PbgP3 protein; 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. (660 aa)    
Predicted Functional Partners:
pbgP2
PbgP2 protein; 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 (By similarity). Essential for virulence in insects; Belongs to the glycosyltransferase 2 family.
 
 0.998
pbgP1
PbgP1 protein; 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.
 
 
 0.992
plu2500
UDP-glucose 6-dehydrogenase; Unnamed protein product; Highly similar to probable nucleotide sugar dehydrogenase and UDP-glucose dehydrogenase.
 
 0.975
pbgP4
PbgP4 protein; 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.
 
  
 0.947
pbgE1
PbgE1 protein; 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 (By similarity).
 
  
 0.938
plu2644
Formyl_trans_N domain-containing protein; Unnamed protein product; Similar to peptide synthetase.
 
  
 
0.912
plu2499
NAD(P)-bd_dom domain-containing protein; Unnamed protein product; Similar to unknown protein WbnF of Escherichia coli and to nucleotide sugar epimerase.
    
 
0.900
pbgE2
PbgE2 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.
 
  
 0.887
rpsL
Ribosomal protein S12; With S4 and S5 plays an important role in translational accuracy.
   
 0.804
rpsS
30S ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
  
 0.790
Your Current Organism:
Photorhabdus laumondii
NCBI taxonomy Id: 243265
Other names: P. laumondii subsp. laumondii TTO1, Photorhabdus laumondii subsp. laumondii TTO1, Photorhabdus luminescens subsp. laumondii TTO1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.