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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
estASecreted alkaliphilic lipase; Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups (212 aa)    
Predicted Functional Partners:
Uncharacterized protein; Belongs to the RBBP9 family
Processive 1,2-diacylglycerol beta-glucosyltransferase; Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta- monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O- (beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D- glucopy [...]
Carboxylesterase; Involved in the detoxification of xenobiotics. Shows maximal activity with C6 substrates, with gradually decreasing activity from C8 to C12 substrates. No activity for higher chain length substrates acids rather than long-chain ones (By similarity)
Diacylglycerol kinase (atp); Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. Is more active toward long-chain DAG compared with short-chain DAG. Is not able to phosphorylate substrates other than DAG, such as monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or sphingosine
Carboxylesterase ybfk; Shows carboxylesterase activity in vitro
Carboxylesterase nap; Belongs to the AB hydrolase superfamily
Extracellular esterase estb; An esterase which preferentially hydrolyzes triacylglyceride substrates with short chain fatty acids (less than C10) with the maximum activity towards tricaprylin (C8:0). Active against p- nitrophenylesters with fatty acid chain lengths from C6 to C18
Biofilm hydrophobic layer component; Involved in biofilm formation Self-polymerizes and forms a layer on the surface of biofilms that confers hydrophobicity to the biofilm The layer is stable and capable of resistance to high mechanical force compression . Required for complex colony architecture . May function synergistically with exopolysaccharides and TasA amyloid fibers to facilitate the assembly of the biofilm matrix
Putative long-chain fatty-acid-coa ligase; May be involved in fatty acid metabolism
Promiscuous acetyl xylan esterase-cephalosporin c deacetylase; Esterase that removed acetyl groups from a number of O- acetylated small substrates, such as acetylated xylose, short xylooligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan. Cannot cleave amide linkages
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, 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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