ID   PLSY_GEOSL              Reviewed;         194 AA.
AC   P60926;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=GSU0507;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR33838.1; -; Genomic_DNA.
DR   RefSeq; NP_951565.1; NC_002939.5.
DR   RefSeq; WP_010941175.1; NC_002939.5.
DR   AlphaFoldDB; P60926; -.
DR   SMR; P60926; -.
DR   STRING; 243231.GSU0507; -.
DR   EnsemblBacteria; AAR33838; AAR33838; GSU0507.
DR   KEGG; gsu:GSU0507; -.
DR   PATRIC; fig|243231.5.peg.508; -.
DR   eggNOG; COG0344; Bacteria.
DR   HOGENOM; CLU_081254_7_1_7; -.
DR   InParanoid; P60926; -.
DR   OMA; WRHRGNL; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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..194
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000188374"
FT   TRANSMEM        4..24
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        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        137..157
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   194 AA;  20149 MW;  42628DD1DA515780 CRC64;
     MLNELILTAV AYIVGSIPTG LLLARASGVD IRATGSGNIG ATNVYRTLGR TVGIATLLGD
     CLKGLVPVLV ARKLGFADPW VAAVGLAAFL GHVYTIFLGF KGGKGVATAL GVFLGVSPLS
     VLGALALFIG IVATTRYISL GSIIAAAAMP LFVAAVERRP LLVGMTLVIA VIVIVKHREN
     IRRLREGTEN RFKA