STRINGSTRING
yybI yybI sspB sspB sigG sigG sigF sigF spoIIAB spoIIAB spoIIM spoIIM spoIVB spoIVB spoIIIAH spoIIIAH tasA tasA spoIVCA spoIVCA lonA lonA gerE gerE tgl tgl cotB cotB cotG cotG spoIIID spoIIID spoIIQ spoIIQ spoIID spoIID spoIIR spoIIR rsfA rsfA yaaH yaaH csfB csfB gcaD gcaD spoVT spoVT amyE amyE sspE sspE gerR gerR
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Network nodes represent proteins
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
Others
textmining
co-expression
protein homology
Your Input:
yybIInner spore coat protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (262 aa)
sspBSmall acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. (67 aa)
sigGRNA polymerase sporulation-specific sigma factor (sigma-G); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes in the forespore. (260 aa)
sigFRNA polymerase sporulation-specific sigma factor (sigma-F); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes. Interaction with SpoIIAB inhibits sigma-F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma F activity is released in the prespore. Responsible for expression of csfB (the anti-sigma-G factor Gin). (255 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)
spoIIMAutolysin component for dissolution of the septal cell wall (stage II sporulation); Required for complete septum migration and engulfment of the forespore compartment during sporulation. Required for stabilizing and recruiting of SpoIIP to the septal membrane. (214 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)
spoIIIAHStage III sporulation ratchet engulfment protein; Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling. (218 aa)
tasAMajor biofilm matrix component; TasA is the major protein component of the biofilm extracellular matrix. It forms amyloid fibers that bind cells together in the biofilm. Exhibits an antibacterial activity against a variety of Gram-positive and Gram-negative bacteria. In laboratory strains, is also involved in proper spore coat assembly. (261 aa)
spoIVCARNA polymerase sporulation-specific sigma-K factor precursor (Sigma-27) (N-terminal half); Putative site-specific recombinase having a very important role in sporulation. It probably plays a role in the recombination of SpoIIIC and SpoIVCB to form sigma K factor. (500 aa)
lonAClass III heat-shock ATP-dependent LonA protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). Has been implicated in preventing sigma(G) activity under non-sporulation conditions. (774 aa)
gerETranscriptional regulator; Involved in the regulation of spore formation. Directs the transcription of several genes that encode structural components of the protein coat that encases the mature spore (CotB, CotC, CotG, CotS, CotV, CotW, CotX, CotY and CotZ). Controls also the cgeAB and cgeCDE operons. (74 aa)
tglProtein-glutamine gamma-glutamyltransferase (transglutaminase); Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of GerQ in higher molecular mass forms, probably in cooperation with YabG; Belongs to the bacillus TGase family. (245 aa)
cotBSpore coat protein (outer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (380 aa)
cotGSpore morphogenetic protein; May be a morphogenetic protein that is required for the incorporation of protein CotB into the spore coat. (195 aa)
spoIIIDTranscriptional regulator; This protein regulates the transcription of sigK, which encodes mother cell chamber RNA polymerase sigma-factor (sigma K). (93 aa)
spoIIQForespore protein required for alternative engulfment; Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling. (283 aa)
spoIIDAutolysin required for complete dissolution of the asymmetric septum (stage II sporulation); May act at the level of sigma-G activity or its stability. SpoIID is probably required for engulfment. (343 aa)
spoIIRpro-sigma(E) endopeptidase (stage II sporulation); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (224 aa)
rsfAPrespore-specific regulatory gene; Seems to improve the efficiency of sporulation by fine-tuning the expression of genes in the sigma F regulon, particularly the timing of their expression. Negatively regulates spoIIR and its own synthesis. (258 aa)
yaaHSpore peptidoglycan hydrolase; N-acetylglucosaminidase involved in cortex peptidoglycan degradation during germination. Cleaves only partially degraded spore peptidoglycans. Recognizes muramic acid delta-lactam residues specific to spore peptidoglycans. (427 aa)
csfBForespore-specific anti-sigma factor; An anti-sigma-G factor, prevents premature activation of sigma-G factor in the forespore; overexpression leads to 1000-fold reduction in spore formation, spore formation stops after engulfment. Overexpression also inhibits sigma- G transcription activation activity. When both Gin and sigma-G are expressed in E.coli Gin inhibits sigma-G, strongly suggesting Gin inhibits by direct physical interaction. (64 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)
spoVTTranscriptional regulator; Transcriptional factor that regulates positively or negatively the expression of a large number of forespore-specific sigma G-dependent genes. May provide a mechanism of feedback control that is important for forespore development. SpoVT levels during spore formation have a major impact on the germination and the resistance of the resultant spores. To B.subtilis AbrB and Abh. (178 aa)
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 aa)
sspESmall acid-soluble spore protein (gamma-type SASP); SASP are proteins degraded in the first minutes of spore germination and provide amino acids for both new protein synthesis and metabolism. These proteins may be involved in dormant spore's high resistance to UV light. (84 aa)
gerRDNA-binding regulator; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type r: regulator. (193 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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