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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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
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[Homology]
Score
fabZ3-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. (151 aa)    
Predicted Functional Partners:
lpxA
UDP-N-acetylglucosamine acyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
 
 0.994
KFX05890.1
Polyketide synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.966
accA
acetyl-CoA carboxylase subunit alpha; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
 
 
 0.941
lpxC
UDP-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.
   
 0.934
lpxD
UDP-3-O-(3-hydroxymyristoyl) glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O- (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-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.
 
 
 0.931
KFX07876.1
Malonyl CoA-ACP transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.930
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.
 
  
 0.925
KFX03244.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.911
fabH
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family.
 
  
 0.907
KFX03814.1
3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.906
Your Current Organism:
Pectobacterium betavasculorum
NCBI taxonomy Id: 55207
Other names: ATCC 43762, CFBP 2122, CIP 105193, DSM 18076, Erwinia carotovora subsp. betavasculorum, ICMP 4226, LMG 2464, LMG 2466, LMG:2464, LMG:2466, NCPPB 2795, P. betavasculorum, Pectobacterium carotovorum subsp. betavasculorum, UCPB 193
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