STRINGSTRING
cotW cotW yaaH yaaH amyE amyE yhaX yhaX cotZ cotZ cotY cotY cotX cotX cotT cotT spoVM spoVM cotE cotE cotM cotM yoaN yoaN cotD cotD spoIVA spoIVA safA safA spoVID spoVID ytxO ytxO cotS cotS yuzC yuzC cotG cotG
Nodes:
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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:
cotWSpore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (105 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)
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 aa)
yhaXPutative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (288 aa)
cotZSpore coat protein (insoluble fraction, outermost layer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (148 aa)
cotYOuter spore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (162 aa)
cotXSpore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (172 aa)
cotTSpore coat protein (inner coat); Inner spore coat protein which seems to play a role in germination. (82 aa)
spoVMFactor required for normal spore cortex and coat synthesis (stage V sporulation); Coordinates cortex and coat assembly during sporulation. Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface. May also serve as a competitive inhibitor of FtsH activity during sporulation. (26 aa)
cotEMorphogenic spore protein; Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins. (181 aa)
cotMSpore coat protein (outer); Involved in spore outer coat assembly. May be part of a cross-linked insoluble skeleton that surrounds the spore, serves as a matrix for the assembly of additional outer coat material, and confers structural stability to the final structure. (130 aa)
yoaNOxalate decarboxylase; Converts oxalate to formate and CO(2); To B.subtilis OxdC. (392 aa)
cotDSpore coat protein (inner); Evidence 1a: Function experimentally demonstrated in the studied strain; cell process. (75 aa)
spoIVAMorphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM. (492 aa)
safAMorphogenetic protein associated with SpoVID; Probably involved in the assembly of some coat protein components implicated in both lysozyme resistance and germination. Could be required for the assembly of CotG. Associates with SpoIVD during the early stage of coat assembly. (387 aa)
spoVIDMorphogenetic spore protein (stage VI sporulation); Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore. (575 aa)
ytxOOuter spore coat protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (143 aa)
cotSSpore coat protein; Seems to be required for the assembly of the CotSA protein in spores. (351 aa)
yuzCInner spore coat protein; Evidence 2b: Function of strongly homologous gene; Product type cp: cell process. (122 aa)
cotGSpore morphogenetic protein; May be a morphogenetic protein that is required for the incorporation of protein CotB into the spore coat. (195 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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