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yhxC yhxC cotZ cotZ cotY cotY cotX cotX ykvN ykvN spoVFA spoVFA spoVFB spoVFB cotE cotE cotU cotU cotC cotC sodF sodF spoIVA spoIVA ypeB ypeB sleB sleB spmB spmB spmA spmA sodA sodA safA safA spoVID spoVID ytfJ ytfJ sspA sspA cotS cotS cotSA cotSA cotB cotB cotG cotG yqiG yqiG yaaH yaaH sspF sspF alrA alrA ydhD ydhD cotJA cotJA cotJB cotJB cotJC cotJC yhcQ yhcQ yhaX yhaX
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:
yhxCPutative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (285 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)
ykvNPutative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (118 aa)
spoVFASpore dipicolinate synthase subunit A; Together with DpaB, catalyzes the conversion of dihydrodipicolinate to dipicolinate (DPA), which constitutes up to 10% of the dry weight of the spore. (297 aa)
spoVFBSpore dipicolinate synthase subunit B; Together with DpaA, catalyzes the conversion of dihydrodipicolinate to dipicolinate (DPA), which constitutes up to 10% of the dry weight of the spore. (200 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)
cotUSpore coat protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor. (86 aa)
cotCSpore coat protein (outer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (66 aa)
sodFSuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. (281 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)
ypeBSpore membrane component; Required for spore cortex hydrolysis during germination. Appears to be required for either expression, localization, activation or function of SleB. (450 aa)
sleBSpore cortex-lytic enzyme; Could be a lytic transglycosylase. Required for spore cortex hydrolysis during germination. Interacts strongly but noncovalently with spore components. (305 aa)
spmBSpore maturation protein; Involved in spore core dehydration; might be involved in the transport of something into or out of the forespore or could be required for some modification of the cortex peptidoglycan structure; Belongs to the SpmB family. (178 aa)
spmASpore maturation protein; Involved in spore core dehydration; might be involved in the transport of something into or out of the forespore or could be required for some modification of the cortex peptidoglycan structure. (196 aa)
sodASuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family. (202 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)
ytfJConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (151 aa)
sspASmall acid-soluble spore protein (alpha-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. (69 aa)
cotSSpore coat protein; Seems to be required for the assembly of the CotSA protein in spores. (351 aa)
cotSASpore coat protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process; Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily. (377 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)
yqiGPutative NADH-dependent flavin oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. (372 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)
sspFSmall acid-soluble spore protein (alpha/beta-type SASP); May play some important role in either sporulation or the dormant spore. (61 aa)
alrAD-alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (389 aa)
ydhDSpore cortex lytic enzyme; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type cp: cell process; Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. (420 aa)
cotJAComponent of the inner spore coat; The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat. (82 aa)
cotJBComponent of the inner spore coat; The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat. (87 aa)
cotJCComponent of the inner spore coat; The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat. (189 aa)
yhcQConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (217 aa)
yhaXPutative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (288 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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