yvoF

Gene Description

YvoF is a membrane-associated, acetyl-CoA-dependent O-acetyltransferase that acetylates the free glyceryl hydroxyl groups of heptaprenylglycerol in Bacillus subtilis. It produces acetylated ether lipids that supply acetyl groups to the lipoprotein N-acetyltransferase LhaT. YvoF loads the lipid carrier on the cytoplasmic side of the membrane; it does not itself acetylate the lipoprotein amino terminus. Its attachment to the membrane and the mechanism by which the carrier crosses the bilayer remain unresolved.

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0016407 acetyltransferase activity	IBA GO_REF:0000033	MODIFY	Summary: YvoF catalyzes O-acetylation of the glyceryl headgroup of an ether-lipid acetyl carrier. Reason: The inherited acetyltransferase claim is supported by target-gene deletion/complementation and recombinant enzyme chemistry. The acceptor atoms are glyceryl oxygens, so refine GO:0016407 to its O-acetyltransferase descendant GO:0016413. This is increased chemical specificity, not rejection of PAINT ancestry or inference from donor count. The required PAINT lineage check found no IRD or IKR loss. The 2016 primary identifies the acetyl-CoA-dependent YvoF reaction, and the 2025 reconstitution uses YvoF to generate an acetylated geranylgeranyl analogue of native HepG. Similarity to maltose O-acetyltransferase does not establish maltose as a physiological substrate; the 2016 study reports that MAT fails to complement the yvoF deletion. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN001917401 SUPPORTS TRANSFER The inherited generic acetyltransferase claim is consistent with target biochemical evidence. The lineage-loss check found no IRD/IKR; no ancestral-node placement error is asserted. Refinement specifies the directly supported oxygen acceptor rather than rejecting the transfer or treating the extant donor list as a similarity score. Proposed replacements: O-acetyltransferase activity Supporting Evidence: PMID:27226549 The acetyl-CoA-dependent enzyme YvoF is a close relative of maltose O-acetyltransferase (MAT). PMID:40626731 which is subsequently dephosphorylated by a non-specific phosphatase prior to acetylation by YvoF to form acetylated heptaprenylglyceryl (Ac-HepG) with acetyl-coenzyme A (Ac-CoA) as donor PMID:40626731 We substituted the commercially available geranylgeranyl pyrophosphate (GGPP) (four isoprenyl repeats) for the native heptaprenyl pyrophosphate (seven isoprenyl repeats) carrier

Core Functions

Acetyl-CoA-dependent O-acetylation of HepG glyceryl hydroxyls to supply acetylated lipid donor for LhaT. Membrane association is supported by activity fractionation; cytoplasmic-side loading follows donor accessibility and the pathway model. The 2025 reconstitution uses a shorter geranylgeranyl lipid analogue.

Molecular Function:

O-acetyltransferase activity

Cellular Locations:

plasma membrane

Supporting Evidence:

PMID:27226549
The acetyl-CoA-dependent enzyme YvoF is a close relative of maltose O-acetyltransferase (MAT).
PMID:40626731
which is subsequently dephosphorylated by a non-specific phosphatase prior to acetylation by YvoF to form acetylated heptaprenylglyceryl (Ac-HepG) with acetyl-coenzyme A (Ac-CoA) as donor
file:BACSU/yvoF/yvoF-source-analysis/PMID27226549-reading.md
No activity was left in the fraction of soluble proteins.

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

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