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minJ minJ htrB htrB spoIVB spoIVB htrC htrC htrA htrA ylbL ylbL rseP rseP ctpA ctpA ctpB ctpB
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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:
minJTopological determinant of cell division; The main function of the Min system is to promote the disassembly of the cytokinetic ring after cell division, thereby ensuring that division occurs only once per cell cycle. MinJ acts as a bridge between DivIVA and MinD. May modulate activity and localization of MinD and MinC through direct interaction with MinD. (397 aa)
htrBHtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (458 aa)
spoIVBRegulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter. (426 aa)
htrCPutative sensor protein; Evidence 7: Gene remnant; Product type pr: putative regulator. (400 aa)
htrAMembrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (449 aa)
ylbLPutative degradative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (341 aa)
rsePRegulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. (422 aa)
ctpACarboxy-terminal processing protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (466 aa)
ctpBSwarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family. (480 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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