⊟Summary[edit | edit source]
- pan ID?: SAUPAN003921000
- symbol?: —
- synonym:
- description?: membrane protein
- membrane protein
- DUF1405 domain-containing protein
- hypothetical protein with DUF1405
- membrane spanning protein
- putative transmembrane protein
- YpjA
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4242365..4242673
- synteny block?: BlockID0029670
- occurrence?: in 100% of 34 strains
lhaT (ypjA) : diacyl-lipoprotein heptaprenylglyceryl N-acetyltransferase LhaT [1]
The PcrB-YvoF-LhaT system provides activated acetyl groups to protect exposed amino termini of extracellular lipoproteins from oxidative damage. LhaT is an integral membrane protein that transfers activated acetyl groups from heptaprenyl carrier units to exposed amino termini of exolipoproteins. 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 MTIKAFWQYTLYQRSWLMMLLICNILGMIYGYIWYGEQLSHTPWHFKIFVPDSPTAILYL
N315 MTINTFWQYTLYQRSWLMMLLICNILGMIYGYIWYGEQLSHTPWHFKIFVPDSPTAILYL
NCTC8325 MTIKAFWQYTLYQRSWLMMLLICNILGMIYGYIWYGEQLSHTPWHFKIFVPDSPTAILYL
Newman MTIKAFWQYTLYQRSWLMMLLICNILGMIYGYIWYGEQLSHTPWHFKIFVPDSSTAILYL
USA300_FPR3757 MTIKAFWQYTLYQRSWLMMLLICNILGMIYGYIWYGEQLSHTPWHFKIFVPDSPTAILYL
***::************************************************.******
COL VISISLILIQKQNSIIDALAFVTLFKYGIWAVIMNILFIIEQGDITVNGLVLMFSHSIMA
N315 VISISLILIQKQNSIIEALAFVTLFKYGIWAVIMNILFIIEQGDITVNGLVLMFSHSIMA
NCTC8325 VISISLILIQKQNSIIDALAFVTLFKYGIWAVIMNILFIIEQGDITVNGLVLMFSHSIMA
Newman VISISLILIQKQNSIIDALAFVTLFKYGIWAVIMNILFIIEQGDITVNGLVLMFSHSIMA
USA300_FPR3757 VISISLILIQKQNSIIDALAFVTLFKYGIWAVIMNILFIIEQGDITVNGLVLMFSHSIMA
****************:*******************************************
COL VQAIYFYPRFKRSMIGISVAMIWVFLNDYIDYFHLQFPYYDFITTHVWQIGVLSCCLSVF
N315 VQAIYFYPRFKRSMIGISVAMIWVFLNDYIDYFHLQFPYYDFITTHVWQIGVLSCCLSVF
NCTC8325 VQAIYFYPRFKRSMIGISVAMIWVFLNDYIDYFHLQFPYYDFITTHVWQIGVLSCCLSVF
Newman VQAIYFYPRFKRSMIGISVAMIWVFLNDYIDYFHLQFPYYDFITTHVWQIGVLSCCLSVF
USA300_FPR3757 VQAIYFYPRFKRSMIGISVAMIWVFLNDYIDYFHLQFPYYDFITTHVWQIGVLSCCLSVF
************************************************************
COL GLLLYIELNKLLKCK
N315 GLLLYIELNKLLKCK
NCTC8325 GLLLYIELNKLLKCK
Newman GLLLYIELNKLLKCK
USA300_FPR3757 GLLLYIELNKLLKCK
***************
- ↑ Alex Reed, Timothy Ware, Haoxin Li, J Fernando Bazan, Benjamin F Cravatt
TMEM164 is an acyltransferase that forms ferroptotic C20:4 ether phospholipids.
Nat Chem Biol: 2023, 19(3);378-388
[PubMed:36782012] [WorldCat.org] [DOI] (I p)John H Gardiner, Gloria Komazin, Miki Matsuo, Kaitlin Cole, Friedrich Götz, Timothy C Meredith
Lipoprotein N-Acylation in Staphylococcus aureus Is Catalyzed by a Two-Component Acyl Transferase System.
mBio: 2020, 11(4);
[PubMed:32723923] [WorldCat.org] [DOI] (I e)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)