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yfkJ yfkJ phoB phoB ysaA ysaA yqfL yqfL fliY fliY prpC prpC suhB suhB phoA phoA ywlE ywlE ppaX ppaX uppP uppP
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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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experimentally determined
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gene co-occurrence
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textmining
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Your Input:
yfkJProtein-tyrosine-phosphatase; Dephosphorylates the phosphotyrosine-containing proteins. Involved in ethanol stress resistance. (156 aa)
phoBAlkaline phosphatase III; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family. (462 aa)
ysaAPutative phosphatase; Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro; Belongs to the HAD-like hydrolase superfamily. (260 aa)
yqfLPositive regulator of gluconeogenesis; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. (270 aa)
fliYFlagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. (378 aa)
prpCPhosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. (254 aa)
suhBInositol monophosphatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the inositol monophosphatase superfamily. (265 aa)
phoAAlkaline phosphatase A; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family. (461 aa)
ywlEProtein-tyrosine-phosphatase; Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved i [...] (150 aa)
ppaXP-Ser-HPr phosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool; Belongs to the HAD-like hydrolase superfamily. PpaX family. (216 aa)
uppPUndecaprenyl-diphosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family. (276 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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