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cotZ cotZ spoVM spoVM yabG yabG yaaH yaaH cotM cotM cotE cotE spoIVA spoIVA spoVID spoVID yuzC yuzC lytH lytH
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.
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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:
cotZSpore coat protein (insoluble fraction, outermost layer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (148 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)
yabGSporulation-specific protease; Cleaves the spore coat proteins SpoIVA and SafA. May cooperate with tgl to mediate the temperature-dependent cross-linking of coat proteins like GerQ. (290 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)
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)
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)
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)
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)
yuzCInner spore coat protein; Evidence 2b: Function of strongly homologous gene; Product type cp: cell process. (122 aa)
lytHSporulation-specific L-Ala-D-Glu endopeptidase; L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation. (326 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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