PLSY_STRT1
ID PLSY_STRT1 Reviewed; 213 AA.
AC Q5M0R8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=str0587;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01043};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
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DR EMBL; CP000024; AAV62183.1; -; Genomic_DNA.
DR RefSeq; WP_002950167.1; NC_006449.1.
DR AlphaFoldDB; Q5M0R8; -.
DR SMR; Q5M0R8; -.
DR GeneID; 66898491; -.
DR KEGG; stc:str0587; -.
DR HOGENOM; CLU_081254_0_0_9; -.
DR OMA; WRHRGNL; -.
DR UniPathway; UPA00085; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..213
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188472"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 213 AA; 23236 MW; 68D0FC7DD69AC1C1 CRC64;
MKILLLILIA YLLGSIQTGL WIGKVFFHTN LREHGSGNTG TTNTFRVLGK TAGTITFLVD
MLKGTLAVLL PIWLGVTEVS PLIIGFFAII GHVFPFFTGF KGGKAVATSA GVLLGFVPLY
FVFLLLVFAL TLYLTSMISF SSITAAVVGL ITLATFPAIH FLLDGYDPIF SAVLIIIALV
IIFRHTENIA RIRNHRENLV PFGLNLTKQN PNK
