ID   PLSY_CERSK              Reviewed;         201 AA.
AC   B9KNF0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
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};
GN   OrderedLocusNames=RSKD131_2396;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
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}.
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DR   EMBL; CP001150; ACM02256.1; -; Genomic_DNA.
DR   RefSeq; WP_009563048.1; NC_011963.1.
DR   AlphaFoldDB; B9KNF0; -.
DR   SMR; B9KNF0; -.
DR   EnsemblBacteria; ACM02256; ACM02256; RSKD131_2396.
DR   GeneID; 57471336; -.
DR   GeneID; 67447776; -.
DR   KEGG; rsk:RSKD131_2396; -.
DR   HOGENOM; CLU_081254_1_0_5; -.
DR   OMA; WRHRGNL; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001597; Chromosome 1.
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 inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..201
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000149580"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ   SEQUENCE   201 AA;  20589 MW;  736C4698FDB14522 CRC64;
     MPAIESGLWA LILTGVLGYL LGSIPFGIVI TRALGLGDLR KIGSGNIGAT NVLRTGNKPA
     ALATLLLDSG KGAIAVLIAR AAVGEDAAQL AAFTSFLGHL FPVWLGFRGG KGVATFLGTL
     LALAWPVGLA CCLTWLATAA LGRISSLSAL VAAASGVLWM ILLGYGQMAA LGAVLAVLIF
     IRHHANIRRI LAGTEPRIGK K