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PLSY_SALTI
ID   PLSY_SALTI              Reviewed;         203 AA.
AC   P67162; Q8XGX7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=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=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_01043};
DE            EC=2.3.1.n5 {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}; Synonyms=ygiH;
GN   OrderedLocusNames=STY3386, t3127;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to
CC       glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This
CC       enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl-
CC       PO(4). {ECO:0000255|HAMAP-Rule:MF_01043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01043};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC         glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42300, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:57970, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC         EC=2.3.1.n5; Evidence={ECO:0000255|HAMAP-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; AL513382; CAD07732.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70670.1; -; Genomic_DNA.
DR   RefSeq; NP_457598.1; NC_003198.1.
DR   RefSeq; WP_001272784.1; NZ_WSUR01000003.1.
DR   AlphaFoldDB; P67162; -.
DR   SMR; P67162; -.
DR   STRING; 220341.16504284; -.
DR   EnsemblBacteria; AAO70670; AAO70670; t3127.
DR   KEGG; stt:t3127; -.
DR   KEGG; sty:STY3386; -.
DR   PATRIC; fig|220341.7.peg.3447; -.
DR   eggNOG; COG0344; Bacteria.
DR   HOGENOM; CLU_081254_0_2_6; -.
DR   OMA; WRHRGNL; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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:InterPro.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
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..203
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000188441"
FT   TOPO_DOM        1..3
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TOPO_DOM        25..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TOPO_DOM        74..80
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TOPO_DOM        102..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TOPO_DOM        133..137
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT   TOPO_DOM        159..203
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ   SEQUENCE   203 AA;  21904 MW;  111ED9CCD73B1D27 CRC64;
     MSAIAPGMIL FAYLCGSISS AILVCRIAGL PDPRESGSGN PGATNVLRIG GKGAAVAVLI
     FDILKGMLPV WGAYALGVTP FWLGLIAIAA CLGHIWPVFF GFKGGKGVAT AFGAIAPIGW
     DLTGVMAGTW LLTVLLSGYS SLGAIVSALI APFYVWWFKP QFTFPVSMLS CLILLRHHDN
     IQRLWRRQET KIWTKLKKKR QKD
 
 
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