PLSY_STRGC
ID PLSY_STRGC Reviewed; 214 AA.
AC Q9X972; A8AXM0;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 116.
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=SGO_1246;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RX PubMed=10525836; DOI=10.1007/s002849900466;
RA Vriesema A.J., Dankert J., Zaat S.A.;
RT "Isolation and characterization of promoter regions from Streptococcus
RT gordonii CH1.";
RL Curr. Microbiol. 39:321-326(1999).
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; CP000725; ABV09391.1; -; Genomic_DNA.
DR EMBL; AJ236899; CAB40549.1; -; Genomic_DNA.
DR RefSeq; WP_012000642.1; NC_009785.1.
DR AlphaFoldDB; Q9X972; -.
DR SMR; Q9X972; -.
DR STRING; 467705.SGO_1246; -.
DR EnsemblBacteria; ABV09391; ABV09391; SGO_1246.
DR GeneID; 61440624; -.
DR KEGG; sgo:SGO_1246; -.
DR eggNOG; COG0344; Bacteria.
DR HOGENOM; CLU_081254_0_0_9; -.
DR OMA; WRHRGNL; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001131; Chromosome.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..214
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188462"
FT TRANSMEM 8..28
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 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT CONFLICT 56
FT /note="V -> D (in Ref. 2; CAB40549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23299 MW; E901CE4150EC577A CRC64;
MINTILGLIL AYLLGSIPTG LWIGQIFFKK NLREYGSGNT GTTNTFRILG KTAGTVTFAI
DFLKGTLATL LPLFLHINGI SPMIFGLIAV LGHTFPIFAE FKGGKAVATS AGVVLGFSPL
FFSYLIIIFI VTLYLGSMIS LASIVVAGFA IISVLIFPLL GIILPSYDLL FTLIIILLAS
IILIRHRDNM ERIKNKSENL IPWGINITKQ VPKK
