Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis.
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B. subtilis PlsC uses acyl-ACP and not acyl-CoA as acyl donor, and depletion of PlsC stops phospholipid synthesis while fatty acid synthesis continues, with fatty acids accumulating from dephosphorylation of 1-acylglycerol-3-phosphate.
"whereas PlsC used only acyl-ACP as an acyl donor"
Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli.
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A plsC temperature-sensitive strain accumulates 1-acyl-G3P and makes no phospholipid at the restrictive temperature, confirming PlsC as the 1-acyl-G3P acyltransferase of B. subtilis.
"At the restrictive temperature, however, 1-acyl-G3P accumulation was observed, and phospholipid synthesis did not take place (Figure 3B)."
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plsC (yhdO) is among the genes that are indispensable for growth when inactivated singly, as reported in the B. subtilis essential gene survey.
"we showed that 271 genes, including plsC (yhdO) and plsX, when inactivated singly, were indispensable for growth in LB medium"
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes.
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GFP fusions place the B. subtilis lipid synthases, including 1-acyl-glycerol-3-phosphate acyltransferase, in the septal membranes, which are also enriched in phosphatidylethanolamine.
"The majority of the lipid synthases were also localized in the septal membranes; this includes 1-acyl-glycerol-3-phosphate acyltransferase"
Bacterial lipid synthesizing enzymes PlsY and PlsC utilize both stereo-forms of glycerol-phosphate.
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In a coupled liposome assay, B. subtilis and E. coli PlsC convert both the (R) and the (S) enantiomer of lysophosphatidic acid into phosphatidic acid, with significantly more of the (R) product.
"Interestingly, both PlsC proteins appear to synthesize more (R)-configurated PA than the other stereoform, suggesting that LPA containing the G3P backbone is the preferred substrate."
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The apparent (R) preference of PlsC is confounded by the lower availability of (S)-lysophosphatidic acid, which had to be generated in situ by PlsY, and the coupled system cannot support kinetic analysis.
"Although this seems to indicate that BsPlsC prefers (R)-LPA as substrate, we cannot rule out this result is partially impacted by the lower availability of (S)-LPA."
Chiral analysis of glycerol phosphates - can bacteria biosynthesize heterochiral phospholipid membranes?
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Both glycerol-phosphate enantiomers occur in B. subtilis, and both appear in the glycerol backbone of some phosphatidylglycerol species, which is the in vivo observation that the stereo-alternative activity of PlsY and PlsC is invoked to explain.
"By using chiral chromatography, the presence of both enantiomers in the glycerol backbone of some molecular species of PG was revealed."
Cached PAINT slice for PANTHER family PTHR10434 (AGPAT/PlsC)
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The IBD assertions that generate both IBA rows sit at PTN000046632, whose seeds include E. coli PlsC (P26647) as well as plant, yeast, mouse and human AGPATs, so the node is ancestral to bacteria and eukaryotes rather than eukaryote-specific.
"PTHR10434 PTN000046632 GO:0003841 F IBD false AGI_LocusCode:AT4G30580|MGI:MGI:1914762|MGI:MGI:1932075|SGD:S000002210|UniProtKB:O15120|UniProtKB:P26647|UniProtKB:Q381S0|UniProtKB:Q99943"
UniProtKB entry O07584 (PLSC_BACSU)
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Curated function, donor specificity, catalytic activity with fatty acyl-[ACP] (Rhea:42296), septal membrane location and disruption phenotype, each tied to the primary literature by ECO:0000269.
"This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA."