entfc-q3xx25

Enterococcus faecium (Streptococcus faecium) alpha/beta hydrolase fold AhyD aminoacylphosphatidylglycerol hydrolase

Comment

A conserved hydrolase responsible for the cleavage of aminoacylphosphatidylglycerol (aa-PG hydrolase) in the membrane of Enterococcus faecium. ahyD is located upstream and adjacent to Aminoacylphosphatidylglycerol synthase (rakPGS) in E. faecium (aa-PGs provide bacteria with resistance to a range of antimicrobial compounds and stress conditions). AhyD hydrolyzes Ala-PG and Lys-PG. AhyD act in concert with RakPGS to maintain optimal levels of aa-PG.. Deletion of ahyD or rakPGS resulted in increased susceptibility to bacitracin || Other strains: Enterococcus faecium DO\; CRL1879\; TX0133a01\; ERV168\; 1,231,501\; SD3B-2

Relationship

Family : 6_AlphaBeta_hydrolase

Block : X

Position in NCBI Life Tree : Enterococcus faecium

Molecular evidence

No mutation

No structure

No kinetic

No disease

No inhibitor

Sequence

Peptide

MTDIIVILYT VGDYVKKEKK YAKMPDGSEI YYEKSGQGFP LFLLHGNDGS GRFFSEQVPV LERYYTVYLV DSRGHGRSTN EASMLNFQLM AEDLNTIMLL EKIDQADFLG FSDGANLALV FASSFPKKVH RLILNSGNTL VKGVRFSARV ISNIHYAWVW LLSLFRPSLR KNLLVIKLLL HDIGLTENDL KKINSPTLII VGKKDVIKLK HSLYIAKTIP KASFVLVKEQ GHELARKDPE RFNREVLQFL SET

References

Title : A conserved hydrolase responsible for the cleavage of aminoacylphosphatidylglycerol in the membrane of Enterococcus faecium - Smith_2013_J.Biol.Chem_288_22768
Author(s) : Smith AM , Harrison JS , Sprague KM , Roy H
Ref : Journal of Biological Chemistry , 288 :22768 , 2013
Abstract : Smith_2013_J.Biol.Chem_288_22768
ESTHER : Smith_2013_J.Biol.Chem_288_22768
PubMedSearch : Smith_2013_J.Biol.Chem_288_22768
PubMedID: 23793054
Gene_locus related to this paper: entfc-q3xx25