The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis.
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Original characterization of spoVD gene encoding a sporulation-specific PBP
"The Bacillus subtilis spoVD gene has been cloned and sequenced. It encodes a 71,262 Da protein with extensive sequence similarity to penicillin-binding proteins from various organisms"
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Demonstrated mother-cell-specific expression during sporulation
"SpoVD synthesis probably occurs only in the mother cell since both sigma E and SpoIIID are thought to be specific to this cell type"
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Showed penicillin-binding activity
"Expression of spoVD in E. coli leads to the synthesis of a membrane-associated protein of the size expected for SpoVD, which can bind labelled penicillin"
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Established disruption phenotype (asporogenous, cortex-less spores)
"insertional disruption of the spoVD gene has no effect on vegetative growth or division"
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Determined specialized role in spore cortex morphogenesis
"spoVD seems instead to have a specialized role in the morphogenesis of the spore cortex, which is a modified form of peptidoglycan"
Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation
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SpoVD is a D,D-transpeptidase for cortex peptidoglycan crosslinking
"SpoVD, a nonessential class B penicillin binding protein"
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Forms cognate pair with SpoVE (SEDS glycosyltransferase)
"we have taken advantage of the peptidoglycan synthesis that occurs during sporulation in Bacillus subtilis to examine the interactions between SpoVE, a nonessential, sporulation-specific homolog of the well-conserved and essential SEDS (shape elongation, division, and sporulation) proteins, and SpoVD, a nonessential class B penicillin binding protein"
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Localizes to outer forespore membrane with quantified enrichment
"localization of SpoVD is dependent on SpoVE"
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Catalytic mutants abolish heat-resistant spore formation
"a loss-of-function point mutation in either part of the fusion resulted in loss of function of the entire fusion"
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FRET demonstrates direct SpoVE-SpoVD interaction
"fluorescence resonance energy transfer experiments indicated that SpoVE and SpoVD interact, and co-affinity purification in Escherichia coli demonstrated that this interaction is direct"
Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile
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SpoVE-SpoVD pairs specialized in endospore-formers
"In B. subtilis, SpoVE forms a complex with the sporulation-specific bPBP SpoVD to synthesize a thick protective PG layer known as the cortex during sporulation"
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Comparative phylogenomics shows dedicated sporulation function
"the genes present in the dcw cluster of sporulating Firmicutes likely code for SpoVE and SpoVD, respectively, rather than the canonical cell division proteins FtsW and FtsI"
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SpoVD homologs form divisome-like subcomplex with FtsL/Q/B
"we observed that C. difficile SpoVD interacts with FtsL and FtsQ, suggesting that the ternary sub-complex likely directly regulates the activity of SpoVE-SpoVD"
Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Combined Automated Annotation using Multiple IEA Methods