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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
arnTGlycosyl 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. (555 aa)    
Predicted Functional Partners:
arnD
Polysaccharide 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.
 
 
 0.992
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.
 
  
 0.989
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.
 
  
 0.985
arnE
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 ArnE family.
 
  
 0.966
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.
 
  
 0.955
pagP
Antimicrobial peptide resistance and lipid A acylation PagP; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
  
  
 0.945
Spro_2204
PFAM: sulfatase; protein of unknown function DUF1705; KEGG: yen:YE2150 hypothetical protein.
  
 
 0.943
lpxT
Phosphoesterase PA-phosphatase related; Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1- diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P); Belongs to the LpxT phosphotransferase family.
 
  
 0.931
lpxM
Lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A.
 
  
 0.930
lpxK
Tetraacyldisaccharide 4'-kinase; Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
 
  
 0.928
Your Current Organism:
Serratia proteamaculans
NCBI taxonomy Id: 399741
Other names: S. proteamaculans 568, Serratia proteamaculans 568, Serratia proteamaculans str. 568, Serratia proteamaculans strain 568
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