STRING protein interaction network
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:
some 3D structure is known or predicted
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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
glpDAerobic glycerol-3-phosphate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme (555 aa)    
Predicted Functional Partners:
Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family
Glycerol uptake facilitator protein; Glycerol enters the cell via the glycerol diffusion facilitator protein. This membrane protein facilitates the movement of glycerol across the cytoplasmic membrane; Belongs to the MIP/aquaporin (TC 1.A.8) family
Glycerol uptake operon antiterminator regulatory protein; Regulates expression of the glpD operon. In the presence of glycerol 3-phosphate (G3P) causes antitermination of transcription of glpD at the inverted repeat of the leader region to enhance its transcription. Binds and stabilizes glpD leader mRNA. May also regulate expression of the glpFK operon
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; Belongs to the PlsY family
Glycerol-1-phosphate dehydrogenase [NAD(P)+]; Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species. Prefers NADH over NADPH as coenzyme. Is also able to catalyze the reverse reaction, i.e. the NAD(+)-dependent oxidation of G1P but not of G3P. Does not possess glycerol dehydrogenase activity
Glycerol-3-phosphate dehydrogenase [NAD(P)+]; Involved in the biosynthesis of the sn-glycerol 3- phosphate required for phospholipid synthesis; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family
Phosphate acyltransferase; 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
Glycerol-3-phosphate cytidylyltransferase; Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF; Belongs to the cytidylyltransferase family
1-acyl-sn-glycerol-3-phosphate acyltransferase; Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) by incorporating an acyl moiety at the 2 position. This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA; Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family
Glycerophosphodiester phosphodiesterase; Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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