CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC).
Assays of CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase (CGPTase) (EC 2.7.8.12) in membranes isolated from Bacillus subtilis 168 wild type and 11 strains bearing conditional lethal thermosensitive mutations in tagB, tagD, or tagF revealed that CGPTase deficiency was associated only with mutant tagF alleles. In vitro, thermosensitivity of CGPTase strongly suggests that the structural gene for this enzyme is tagF. We discuss apparent discrepancies between biochemical evidence favoring a membrane location for TagF and a previous report that suggested a cytoplasmic location based on sequence analysis.
Pooley
H M
HM
Institut de Génétique et de Biologie Microbiennes, Lausanne, Switzerland.
Abellan
F X
FX
Karamata
D
D
D001412:Bacillus subtilis / Q000737:chemistry / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D002473:Cell Wall / Q000737:chemistry* / Q000201:enzymology; D005798:Genes, Bacterial; D009876:Operon; D010770:Phosphotransferases / Q000235:genetics* / Q000502:physiology; D013682:Teichoic Acids / Q000096:biosynthesis*; D017855:Transferases (Other Substituted Phosphate Groups)
D001426:Bacterial Proteins; D013682:Teichoic Acids; D010770:Phosphotransferases; D017855:Transferases (Other Substituted Phosphate Groups); C072175:CDP glycerol glycerophosphotransferase