STRINGSTRING
aroA aroA uppP uppP defA defA murE murE defB defB fabI fabI estB estB folB folB gcaD gcaD murAA murAA murAB murAB trmFO trmFO
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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aroA3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvoylshikimate-3-phosphate synthase); Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. (428 aa)
uppPUndecaprenyl-diphosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family. (276 aa)
defAPeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity). (160 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)
defBFormylmethionine deformylase A; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. (184 aa)
fabIEnoyl-acyl carrier protein reductase; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism. (258 aa)
estBSecreted esterase / lipase; 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. (210 aa)
folBDihydroneopterin aldolase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. (120 aa)
gcaDBifunctional glucosamine-1-phosphate N-acetyltransferase/UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belon [...] (456 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)
trmFOtRNA:m(5)U-54 methyltransferase; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. (435 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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