PLSY_HELPY
ID PLSY_HELPY Reviewed; 220 AA.
AC O26039;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043};
DE EC=2.3.1.275 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043};
GN Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043}; OrderedLocusNames=HP_1509;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate
CC (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic
CC acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor,
CC but not acyl-CoA or acyl-ACP. {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01043};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD08551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000511; AAD08551.1; ALT_INIT; Genomic_DNA.
DR PIR; E64708; E64708.
DR RefSeq; NP_208300.1; NC_000915.1.
DR AlphaFoldDB; O26039; -.
DR SMR; O26039; -.
DR STRING; 85962.C694_07815; -.
DR PaxDb; O26039; -.
DR EnsemblBacteria; AAD08551; AAD08551; HP_1509.
DR KEGG; hpy:HP_1509; -.
DR PATRIC; fig|85962.47.peg.1622; -.
DR eggNOG; COG0344; Bacteria.
DR OMA; WRHRGNL; -.
DR PhylomeDB; O26039; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..220
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188381"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 220 AA; 23804 MW; E72004BFF4AB882B CRC64;
MESVLNFLTN INVIFTLLGY LIGGIPFGYA LMKIFYGMDI TKIGSGGIGA TNVLRALQSK
GVSNAKQMAL LVLILDLFKG MFAVFLSKLF GLDYSLQWMV AIASILGHCY SPFLNFNGGK
GVSTIMGSVV LLIPIESLIG LTVWFFVGKV LKISSLASIL GVGTATVLIF FVPYMHIPDS
VNILKEVGTQ TPMVLIFIFT LIKHAGNIFN LLAGKEKKVL
