⊟Summary[edit | edit source]
- pan ID?: SAUPAN004935000
- symbol?: pcrB
- synonym:
- description?: geranylgeranylglyceryl/heptaprenylglyceryl phosphate synthase
- geranylgeranylglyceryl/heptaprenylglyceryl phosphate synthase
- geranylgeranylglyceryl phosphate synthase-like protein
- geranylgeranylglyceryl phosphate synthase
- heptaprenylglyceryl phosphate synthase
- PcrB-like replication protein
- Phosphoglycerol geranylgeranyltransferase
- putative glycerol-1-phosphate prenyltransferase
- (S)-3-O-geranylgeranylglyceryl phosphate synthase
- geranylgeranylglyceryl diphosphate synthase
- geranylgeranylglyceryl phosphate synthase family protein
- PcrB family protein
- PcrB family replication protein
- protein PcrB
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5126096..5126788
- synteny block?: BlockID0038400
- occurrence?: in 100% of 34 strains
pcrB : heptaprenylglyceryl phosphate synthase PcrB [1]
The PcrB-YvoF-LhaT system provides activated acetyl groups to protect exposed amino termini of extracellular lipoproteins from oxidative damage. PcrB catalyzes the initial condensation of heptaprenyl pyrophosphate with glycerol-1-phosphate to generate the heptaprenylglyceryl (HepG) acetyl carrier unit. 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.
• A crystal structure is available: 3W01
⊟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 MYDIKKWRHIFKLDPAKHISDDDLDAICMSQTDAIMIGGTDDVTEDNVIHLMSRVRRYPL
N315 MYDIKKWRHIFKLDPAKHISDDDLDAICMSQTDAIMIGGTDDVTEDNVIHLMSRIRRYPL
NCTC8325 MYDIKKWRHIFKLDPAKHISDDDLDAICMSQTDAIMIGGTDDVTEDNVIHLMSRVRRYPL
Newman MYDIKKWRHIFKLDPAKHISDDDLDAICMSQTDAIMIGGTDDVTEDNVIHLMSRVRRYPL
USA300_FPR3757 MYDIKKWRHIFKLDPAKHISDDDLDAICMSQTDAIMIGGTDDVTEDNVIHLMSRVRRYPL
******************************************************:*****
COL PLVLEISNIESVMPGFDFYFVPTVLNSTDVVFHNGTLLEALKTYGHSIDFEEVIFEGYVV
N315 PLVLEISNIESVMPGFDFYFVPTVLNSTDVAFHNGTLLEALKTYGHSIDFEEVIFEGYVV
NCTC8325 PLVLEISNIESVMPGFDFYFVPTVLNSTDVVFHNGTLLEALKTYGHSIDFEEVIFEGYVV
Newman PLVLEISNIESVMPGFDFYFVPTVLNSTDVVFHNGTLLEALKTYGHSIDFEEVIFEGYVV
USA300_FPR3757 PLVLEISNIESVMPGFDFYFVPTVLNSTDVVFHNGTLLEALKTYGHSIDFEEVIFEGYVV
******************************.*****************************
COL CNADSKVAKHTKANTDLTTEDLEAYAQMVNHMYRLPVMYIEYSGIYGDVSKVQAVSEHLT
N315 CNADSKVAKHTKANTDLTTEDLEAYAQMVNHMYRLPVMYIEYSGIYGDVSKVQAVSEHLT
NCTC8325 CNADSKVAKHTKANTDLTTEDLEAYAQMVNHMYRLPVMYIEYSGIYGDVSKVQAVSEHLT
Newman CNADSKVAKHTKANTDLTTEDLEAYAQMVNHMYRLPVMYIEYSGIYGDVSKVQAVSEHLT
USA300_FPR3757 CNADSKMAKHTKANTDLTTEDLEAYAQMVNHMYRLPVMYIEYSGIYGDVSKVQAVSEHLT
******:*****************************************************
COL ETQLFYGGGISSEQQATEMAAIADTIIVGDIIYKDIKKALKTVKIKESSK
N315 ETQLFYGGGISSEQQATEMAAIADTIIVGDIIYKDIKKALKTVKIKESSK
NCTC8325 ETQLFYGGGISSEQQATEMAAIADTIIVGDIIYKDIKKALKTVKIKESSK
Newman ETQLFYGGGISSEQQATEMAAIADTIIVGDIIYKDIKKALKTVKIKESSK
USA300_FPR3757 ETQLFYGGGISSEQQATEMAAIADTIIVGDIIYKDIKKALKTVKIKESSK
**************************************************
- ↑ 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)