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spo0F spo0F ycgR ycgR rsbU rsbU rsbV rsbV rsbW rsbW rsbP rsbP hag hag hprT hprT rsbX rsbX dprA dprA fliG fliG fliM fliM recA recA lexA lexA ypfA ypfA comEC comEC
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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
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spo0FTwo-component response regulator; Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation. (124 aa)
ycgRPutative permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (294 aa)
rsbUSerine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module. (335 aa)
rsbVAnti-anti-sigma factor (antagonist of RsbW); Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B. (109 aa)
rsbWSwitch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). (160 aa)
rsbPSerine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. (403 aa)
hagFlagellin protein; Flagellin is the subunit which polymerizes to form the filaments of bacterial flagella. Assembly into flagella requires FliW. Acts as a homeostatic autoinhibitory regulator to control its own cytoplasmic levels. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagell [...] (304 aa)
hprTHypoxanthine-guanine phosphoribosyltransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (180 aa)
rsbXSerine phosphatase; Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels. (199 aa)
dprADNA processing Smf single strand binding protein; Protein that helps load RecA onto ssDNA during transformation. Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA. Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments. RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. (297 aa)
fliGFlagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. (338 aa)
fliMFlagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family. (332 aa)
recAMultifunctional SOS repair factor; Multifunctional protein involved in homologous recombination, DNA repair and competence. Can catalyze the hydrolysis of (d)ATP in the presence of single-stranded DNA; prefers dATP at least in vitro, catalyzes the dATP-dependent uptake of single- stranded DNA by duplex DNA, and the dATP-dependent hybridization of homologous single-stranded DNAs (strand exchange). RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. It interacts with LexA causing its activation and leading to its autocatalytic clea [...] (348 aa)
lexATranscriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. (205 aa)
ypfAPutative cyclic diGMP binding protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (217 aa)
comECDNA channel for uptake in competent cells; The comE operon is required for the binding and uptake of transforming DNA. ComEC is required for internalization but is dispensable for DNA binding; To H.influenzae REC2, N.gonorrhoeae ComA and E.coli YcaI. (776 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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