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ddl ddl murF murF alrA alrA spoVD spoVD murE murE mraY mraY murD murD spoVE spoVE murG murG murB murB murC murC murAA murAA murAB murAB pbpG pbpG
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
ddlD-alanyl-D-alanine ligase A; Cell wall formation. (354 aa)
murFUDP-N-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate-D-alanyl-D-alanine ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily. (457 aa)
alrAD-alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (389 aa)
spoVDPenicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. (646 aa)
murEUDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. (494 aa)
mraYphospho-N-acetylmuramoyl-pentapeptide transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily. (324 aa)
murDUDP-N-acetylmuramoylalanyl-D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family. (451 aa)
spoVEFactor for spore cortex peptidoglycan synthesis (stage V sporulation); May play an essential role not only during sporulation, but also during vegetative growth; Belongs to the SEDS family. SpoVE subfamily. (366 aa)
murGUndecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. (363 aa)
murBUDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation. (303 aa)
murCUDP-N-acetyl muramate-alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (432 aa)
murAAUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine. Essential for cell growth; Belongs to the EPSP synthase family. MurA subfamily. (436 aa)
murABUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. (429 aa)
pbpGSporulation specific penicillin-binding protein; Involved in the polymerization and cross-linking of spore peptidoglycan. May be required for synthesis of the spore germ cell wall, the first layer of peptidoglycan synthesized on the surface of the inner forespore membrane; In the C-terminal section; belongs to the transpeptidase family. (691 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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