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:
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.
 
 
 0.985
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.
 
  
 0.984
fabZ
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
    
 0.935
ANW24028.1
D-arabinose 5-phosphate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.862
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.
 
   
 0.855
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).
 
   
 0.849
ANW24215.1
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.
 
   
 0.848
kdsA
3-deoxy-8-phosphooctulonate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the KdsA family.
 
  
 0.844
kdsB
3-deoxy-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
 
   
 0.843
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.
  
  
 0.787
Your Current Organism:
Vibrio coralliilyticus
NCBI taxonomy Id: 190893
Other names: ATCC BAA-450, CAIM 616, LMG 20984, LMG:20984, V. coralliilyticus, Vibrio coralliilyticus Ben-Haim et al. 2003, Vibrio corallilyticus, Vibrio coralyticus, Vibrio sp. LMG 10953, strain YB1
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