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
lpxCUDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis; Belongs to the LpxC family. (305 aa)    
Predicted Functional Partners:
fabZ
(3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
   
 0.965
lpxA
acyl-[acyl-carrier-protein]--UDP-N- acetylglucosamine O-acyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
 
  
 0.938
lpxD
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3- hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
 
 
 0.934
lpxB
lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
 
   
 0.861
EEX35786.1
3-deoxy-D-manno-octulosonic-acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family.
 
   
 0.852
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).
 
   
 0.851
EEX38230.1
Arabinose 5-phosphate isomerase.
 
   
 0.850
kdsB
3-deoxy-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
 
   
 0.841
kdsA
2-Keto-3-deoxy-D-manno-octulosonate-8-phosphate synthase; Belongs to the KdsA family.
 
  
 0.823
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
  
  
 0.797
Your Current Organism:
Vibrio metschnikovii
NCBI taxonomy Id: 675813
Other names: V. metschnikovii CIP 69.14, Vibrio metschnikovii CIP 69.14, Vibrio metschnikovii str. CIP 69.14, Vibrio metschnikovii strain CIP 69.14
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.