⊟Summary[edit | edit source]
- pan ID?: SAUPAN002681000
- symbol?: —
- synonym:
- description?: acetyltransferase
- acetyltransferase
- DapH/DapD/GlmU-related protein
- O-acetyltransferase, putative
- putative acetyltransferase
- bacterial transferase hexapeptide family protein
- hexapaptide repeat-containing transferase
- maltose O-acetyltransferase (Maltose transacetylase). domain protein
- O-acetyltransferase
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 3179570..3180049
- synteny block?: BlockID0019130
- occurrence?: in 100% of 34 strains
yvoF : heptaprenylglyceryl O-acetyltransferase YvoF [1]
The PcrB-YvoF-LhaT system provides activated acetyl groups to protect exposed amino termini of extracellular lipoproteins from oxidative damage. YvoF activates the apo-heptaprenylglyceryl carrier unit with an acetyl group in the cytoplasm after which it is exported and provides a source of high-energy acetyl groups for extracellular modification enzymes such as LhaT. Initially described as a means of protecting exolipoproteins from copper-based oxidative damage in Bacillus, acetylated lipoproteins have not yet been detected from staphylococci suggesting that this system may be nonfunctional or adapted to provide activated acetyl groups to alternative extracellular substrates. Rather than acetylation, the majority of lipoproteins in staphylococci are tri-acylated by the LnsA-LnsB system which reduces their immunorecognition by host TLR2-1/6 receptors.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 | |
| JSNZ |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MRKFLSKTHHHTNPLWRVYRLVKFSKVFKNVIIIEFSKFIPSMVLKRHIYKQLLNINIGN
N315 MRKFLSKTHHHTNPLWRVYRLVKFSKVFKNVIIIEFSKFIPSMVLKRHIYKQLLNINIGN
NCTC8325 MRKFLSKTHHHTNPLWRVYRLVKFSKVFKNVIIIEFSKFIPSMVLKRHIYKQLLNINIGN
Newman MRKFLSKTHHHTNPLWRVYRLVKFSKVFKNVIIIEFSKFIPSMVLKRHIYKQLLNINIGN
USA300_FPR3757 MRKFLSKTHHHTNPLWRVYRLVKFSKVFKNVIIIEFSKFIPSMVLKRHIYKQLLNINIGN
************************************************************
COL QSSIAYKVMLDIFYPELITIGSNSVIGYNVTILTHEALVDEFRYGPVTIGSNTLIGANAT
N315 QSSIAYKVMLDIFYPELITIGSNSVIGYNVTILTHEALVDEFRYGPVTIGSNTLIGANAT
NCTC8325 QSSIAYKVMLDIFYPELITIGSNSVIGYNVTILTHEALVDEFRYGPVTIGSNTLIGANAT
Newman QSSIAYKVMLDIFYPELITIGSNSVIGYNVTILTHEALVDEFRYGPVTIGSNTLIGANAT
USA300_FPR3757 QSSIAYKVMLDIFYPELITIGSNSVIGYNVTILTHEALVDEFRYGPVTIGSNTLIGANAT
************************************************************
COL ILPGITIGDNVKVAAGTVVSKDIPDNGFAYGNPMYIKMIRR
N315 ILPGITIGDNVKVAAGTVVSKDIPDNGFAYGNPMYIKMIRR
NCTC8325 ILPGITIGDNVKVAAGTVVSKDIPDNGFAYGNPMYIKMIRR
Newman ILPGITIGDNVKVAAGTVVSKDIPDNGFAYGNPMYIKMIRR
USA300_FPR3757 ILPGITIGDNVKVAAGTVVSKDIPDNGFAYGNPMYIKMIRR
*****************************************
- ↑ Hartmut Stoll, Jörn Dengjel, Christiane Nerz, Friedrich Götz
Staphylococcus aureus deficient in lipidation of prelipoproteins is attenuated in growth and immune activation.
Infect Immun: 2005, 73(4);2411-23
[PubMed:15784587] [WorldCat.org] [DOI] (P p)Gloria Komazin, Rachel M Wigmore, Aditi M Ranade, Amena A Rizk, John H Gardiner, Timothy C Meredith
Lipoprotein N-terminal modification in Bacillus: a new paradigm for extracellular acetylation and species-dependent Toll-like receptor 2 immunomodulation.
mBio: 2025, 16(8);e0099625
[PubMed:40626731] [WorldCat.org] [DOI] (I p)