PLSY_LEGPH
ID PLSY_LEGPH Reviewed; 277 AA.
AC Q5ZT09;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=lpg2356;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(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 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; AE017354; AAU28418.1; -; Genomic_DNA.
DR RefSeq; WP_010948062.1; NC_002942.5.
DR RefSeq; YP_096365.1; NC_002942.5.
DR AlphaFoldDB; Q5ZT09; -.
DR SMR; Q5ZT09; -.
DR STRING; 272624.lpg2356; -.
DR PaxDb; Q5ZT09; -.
DR PRIDE; Q5ZT09; -.
DR EnsemblBacteria; AAU28418; AAU28418; lpg2356.
DR KEGG; lpn:lpg2356; -.
DR PATRIC; fig|272624.6.peg.2478; -.
DR eggNOG; COG0344; Bacteria.
DR HOGENOM; CLU_081254_0_1_6; -.
DR OMA; WRHRGNL; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000609; 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 inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..277
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188392"
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 79..99
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 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT REGION 207..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 30467 MW; 1D3E520A56C164EF CRC64;
MALFIFLILV GYLMGSINSA IIVCRTFGLP DPREEGSKNP GATNVLRLGG KQYGIMVMVF
DALKGILPVI LAKFLSAEPV TVAFTALAAV VGHMYPVFFH FRGGKGVATT IGALLAFHFI
IGVMVAATWL LVANFWRYSS LASIASISLA PFYSLILVGN LNIFPPLFMI TILVLYKHRD
NFNRLIDGKE PKIKFKHSVI EEIMEASPAT SAEQEFPGKE VIDTNIDETE KTEQAEAVKK
PKVKKATTKA KKTTSKEETT KKPKSTKPKT KTVKEKE
