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
plsXPhosphate acyltransferase PlsX; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. (337 aa)    
Predicted Functional Partners:
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.
 
  
 0.994
plsY
Acyl-phosphate glycerol 3-phosphate acyltransferase; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
 
  
 0.985
OSB10822.1
Fatty acid biosynthesis transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.970
OSB10818.1
Malonyl CoA-acyl carrier protein transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.969
rpmF
50S ribosomal protein L32; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bL32 family.
  
  
 0.918
OSB10815.1
Beta-ketoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
  
  
 0.898
OSB10819.1
2-nitropropane dioxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.820
OSB10824.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.781
OSB10817.1
beta-ketoacyl-ACP reductase; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
  
  
 0.766
rpsM
30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family.
   
    0.764
Your Current Organism:
Paraclostridium bifermentans
NCBI taxonomy Id: 1490
Other names: ATCC 638, BCRC 14542, Bacillus bifermentans, Bacillus bifermentans sporogenes, Bacillus centrosporogenes, CCRC 14542, CCRC:14542, CCUG 36626, CIP 104309, Clostridium bifermentans, DSM 14991, Martellillus bifermentans, NCIMB 10716, NCTC 13019, P. bifermentans
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