PLSY_STRA1
ID PLSY_STRA1 Reviewed; 207 AA.
AC Q3K0U5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=SAK_1244;
OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS SS700).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=205921;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27591 / A909 / CDC SS700;
RX PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA Wessels M.R., Rappuoli R., Fraser C.M.;
RT "Genome analysis of multiple pathogenic isolates of Streptococcus
RT agalactiae: implications for the microbial 'pan-genome'.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
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; CP000114; ABA45851.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3K0U5; -.
DR SMR; Q3K0U5; -.
DR KEGG; sak:SAK_1244; -.
DR HOGENOM; CLU_081254_4_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..207
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188459"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 207 AA; 22832 MW; A50360AAA52971B2 CRC64;
MIIIAYLLGS IQTGLWIGKY FYQVNLRQHG SGNTGTTNTF RILGVKAGIV TLTIDILKGT
LATLIPIILG ITTISPFFIG FFAIIGHTFP IFAQFKGGKA VATSAGVLLG FAPSFFLYLL
VIFLLTLYLF SMISLSSITV AVVGILSVLI FPLVGFILTD YDWIFTTVVI LMALTIIIRH
QDNIKRIRKR QENLVPFGLN LSKQKNK
