Literature summary for 2.3.1.274 extracted from

Sastre, D.; Bisson-Filho, A.; de Mendoza, D.; Gueiros-Filho, F.
Revisiting the cell biology of the acyl-ACP Phosphate transacylase PlsX suggests that the phospholipid synthesis and cell division machineries are not coupled in Bacillus subtilis (2016), Mol. Microbiol., 100, 621-634 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	the enzyme is uniformly distributed on the membrane of most cells, but occasionally appears as membrane foci as well. Foci and homogenous patterns seem freely interconvertible but the prevalence of the uniform staining suggests that PlsX does not need to localize to specific sites to function correctly. PlsX's foci show no obvious periodicity of localization and do not colocalize with the divisome	Bacillus subtilis	-	-

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P71018	-	-
Bacillus subtilis 168 / PY79	P71018	-	-

Synonyms

Synonyms	Comment	Organism
acyl-ACP:phosphate transacylase PlsX	-	Bacillus subtilis

General Information

General Information	Comment	Organism
malfunction	depletion of PlsX does not affect cell division if phospholipid synthesis is maintained by an alternative enzyme	Bacillus subtilis
metabolism	PlsX is a central enzyme of phospholipid synthesis in bacteria, converting acyl-ACP to acyl-phosphate on the pathway to phosphatidic acid formation. PlsX plays a key role in the coordination of fatty acid and phospholipid synthesis	Bacillus subtilis

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Release 2023.1 (January 2023)