STRINGSTRING
cotY cotY amyE amyE cotZ cotZ cotX cotX pyrD pyrD spoVM spoVM cotE cotE cotC cotC cgeA cgeA spoIVA spoIVA lysA lysA spoVID spoVID thrC thrC ganA ganA cotB cotB cotG cotG
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:
cotYOuter spore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (162 aa)
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 aa)
cotZSpore coat protein (insoluble fraction, outermost layer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (148 aa)
cotXSpore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (172 aa)
pyrDDihydroorotate dehydrogenase (catalytic subunit); Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. (311 aa)
spoVMFactor required for normal spore cortex and coat synthesis (stage V sporulation); Coordinates cortex and coat assembly during sporulation. Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface. May also serve as a competitive inhibitor of FtsH activity during sporulation. (26 aa)
cotEMorphogenic spore protein; Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins. (181 aa)
cotCSpore coat protein (outer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (66 aa)
cgeASpore outermost layer component; May be involved in maturation of the outermost layer of the spore. (133 aa)
spoIVAMorphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM. (492 aa)
lysADiaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (439 aa)
spoVIDMorphogenetic spore protein (stage VI sporulation); Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore. (575 aa)
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa)
ganAArabinogalactan type I oligomer exo-hydrolase (beta-galactosidase, lactase); Hydrolyzes oligosaccharides released by the endo-1,4-beta- galactosidase GalA from arabinogalactan type I, a pectic plant polysaccharide. It is unable to use lactose as a sole carbon source. Maximal activity with o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-galactopyranoside (PNPG) as substrates, trace activity with p-nitrophenyl-alpha-L-arabinopyranoside and o- nitrophenyl-beta-D-fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-D-galactopyranoside, p-nitrophenyl [...] (687 aa)
cotBSpore coat protein (outer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (380 aa)
cotGSpore morphogenetic protein; May be a morphogenetic protein that is required for the incorporation of protein CotB into the spore coat. (195 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
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