STRINGSTRING
dhbF dhbF dhbE dhbE dhbC dhbC dhbA dhbA besA besA
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:
dhbFSiderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. (2378 aa)
dhbE2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. (539 aa)
dhbCIsochorismate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the isochorismate synthase family. (398 aa)
dhbA2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (261 aa)
besABacillibactin trilactone hydrolase; Catalyzes the hydrolysis of the trilactone cycle of ferri- bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB. (289 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (36%) [HD]