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yorN yorN amyE amyE ndoA ndoA rnc rnc yosX yosX yosL yosL yorZ yorZ yorM yorM yorE yorE yoqA yoqA yopV yopV yopR yopR yopQ yopQ yopP yopP yopN yopN yopM yopM yonX yonX yonT yonT yonP yonP gapA gapA ganA ganA
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:
yorNHypothetical protein; Evidence 5: No homology to any previously reported sequences. (49 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)
ndoAEndoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U. Yields cleavage products with 3' phosphate and 5' hydroxyl groups. Cannot digest substrate with a UUdUACAUAA cleavage site. Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter. (116 aa)
rncRibonuclease III; Digests double-stranded RNA. Involved in the processing of ribosomal RNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes pre-scRNA (the precursor of the signal recognition particle RNA). Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. (249 aa)
yosXConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (117 aa)
yosLHypothetical protein; Evidence 5: No homology to any previously reported sequences. (117 aa)
yorZHypothetical protein; Evidence 5: No homology to any previously reported sequences. (70 aa)
yorMConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (238 aa)
yorEHypothetical protein; Evidence 5: No homology to any previously reported sequences. (123 aa)
yoqAHypothetical protein; Evidence 5: No homology to any previously reported sequences. (116 aa)
yopVHypothetical protein; Evidence 5: No homology to any previously reported sequences. (64 aa)
yopRPutative integrase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (325 aa)
yopQConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (460 aa)
yopPPutative phage integrase; Probable recombinase that does not seem to have a role in chromosome dimer resolution per se but rather may have some facilitative role during chromosome partitioning in general. Belongs to the 'phage' integrase family. (358 aa)
yopNHypothetical protein; Evidence 5: No homology to any previously reported sequences. (105 aa)
yopMHypothetical protein; Evidence 5: No homology to any previously reported sequences. (66 aa)
yonXConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (168 aa)
yonTHypothetical protein; Evidence 5: No homology to any previously reported sequences. (58 aa)
yonPHypothetical protein; Evidence 5: No homology to any previously reported sequences. (64 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase; Involved in the glycolysis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3- bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. (335 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)
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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