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bpr bpr spoIIE spoIIE aprE aprE kinE kinE spo0E spo0E spoIIAB spoIIAB spoIIAA spoIIAA spo0A spo0A rsh rsh spo0B spo0B phoP phoP sigO sigO spo0F spo0F
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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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bprEvidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (1433 aa)
spoIIESpoIIAA-phosphate serine phosphatase; Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation. (827 aa)
aprESerine alkaline protease (subtilisin E); Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides; Belongs to the peptidase S8 family. (381 aa)
kinETwo-component sensor histidine kinase; Phosphorylates the sporulation-regulatory protein spo0A under biofilm growth conditions. Also able to weakly phosphorylate spo0F. (738 aa)
spo0ENegative regulatory phosphatase acting on Spo0A-P (sporulation); Aspartyl-phosphate phosphatase which specifically dephosphorylates the sporulation transcription factor Spo0A-P and negatively regulates the sporulation initiation pathway in order to control the proper timing of sporulation. Belongs to the spo0E family. (85 aa)
spoIIABAnti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition. (146 aa)
spoIIAAAnti-anti-sigma factor (antagonist of SpoIIAB); In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition; Belongs to the anti-sigma-factor antagonist family. (117 aa)
spo0AResponse regulator; May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box). (267 aa)
rshGTP pyrophosphokinase (RelA/SpoT); In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable); Belongs to the RelA/SpoT family. (734 aa)
spo0BSporulation initiation phosphotransferase; Key element in the phosphorelay regulating sporulation initiation. Acts on spo0A. Mediates reversible phosphoryl transfer from spo0F to spo0A. (192 aa)
phoPTwo-component response regulator; Member of the two-component regulatory system PhoP/PhoR involved in the regulation of alkaline phosphatase genes phoA and phoB and of phosphodiesterase. (240 aa)
sigOAlternative sigma factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Together with its coactivator RsoA, positively regulates the expression of at least three operons, including oxdC-yvrL, sigO-rsoA and yvrJ. Required for the acid stress-dependent induction of the oxalate decarboxylase oxdC. (176 aa)
spo0FTwo-component response regulator; Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation. (124 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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