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
aasacyl-ACP synthetase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. (718 aa)    
Predicted Functional Partners:
lplT
Lysophospholipid transporter LplT; Catalyzes the facilitated diffusion of 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) into the cell; Belongs to the major facilitator superfamily. LplT (TC 2.A.1.42) family.
  
 0.985
pldB
Lysophospholipase L2; Lecithinase B; catalyzes the conversion of 1-lysophosphatidylcholine to glycerophosphocholine; can also hydrolyze 2-acyl glycerophosphoethanolamine and other substrates; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.972
psd
Phosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
    
 0.959
pssA
Catalyzes de novo synthesis of phosphatidylserine from CDP-diacylglycerol and L-serine which leads eventually to the production of phosphatidylethanolamine; bounds to the ribosome; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.955
pldA
Phospholipase A; Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Belongs to the phospholipase A1 family.
     
 0.951
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
  
 0.949
AKA39360.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.949
fadJ
Multifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
  
 0.919
fadB
Multifunctional fatty acid oxidation complex subunit alpha; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
  
 0.919
rplF
50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
    
 0.919
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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