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Database: UniProt/SWISS-PROT
Entry: PLSY_BLOFL
LinkDB: PLSY_BLOFL
Original site: PLSY_BLOFL 
ID   PLSY_BLOFL              Reviewed;         196 AA.
AC   Q7VQQ8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   29-MAY-2013, entry version 63.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase;
DE   AltName: Full=Acyl-PO4 G3P acyltransferase;
DE   AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase;
DE   AltName: Full=G3P acyltransferase;
DE            Short=GPAT;
DE            EC=2.3.1.n3;
DE   AltName: Full=Lysophosphatidic acid synthase;
DE            Short=LPA synthase;
GN   Name=plsY; OrderedLocusNames=Bfl060;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis
RT   of reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
CC   -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-
CC       phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form
CC       lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate
CC       as fatty acyl donor, but not acyl-CoA or acyl-ACP (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1-
CC       acyl-sn-glycerol 3-phosphate + phosphate.
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC   -!- SUBUNIT: Probably interacts with PlsX (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the PlsY family.
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DR   EMBL; BX248583; CAD83585.1; -; Genomic_DNA.
DR   RefSeq; NP_878372.1; NC_005061.1.
DR   STRING; 203907.Bfl060; -.
DR   EnsemblBacteria; CAD83585; CAD83585; Bfl060.
DR   GeneID; 1499260; -.
DR   KEGG; bfl:Bfl060; -.
DR   PATRIC; 31963711; VBICanBlo38691_0061.
DR   eggNOG; COG0344; -.
DR   HOGENOM; HOG000283806; -.
DR   KO; K08591; -.
DR   OMA; WRHRGNL; -.
DR   ProtClustDB; CLSK2411639; -.
DR   BioCyc; BFLO203907:GHF7-60-MONOMER; -.
DR   UniPathway; UPA00085; -.
DR   GO; GO:0016021; C:integral to 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:HAMAP.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01043; PlsY; 1; -.
DR   InterPro; IPR003811; G3P_acylTferase.
DR   Pfam; PF02660; G3P_acyltransf; 1.
DR   TIGRFAMs; TIGR00023; TIGR00023; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    196       Glycerol-3-phosphate acyltransferase.
FT                                /FTId=PRO_0000188331.
FT   TRANSMEM      1     21       Helical; (Potential).
FT   TRANSMEM     55     75       Helical; (Potential).
FT   TRANSMEM     81    101       Helical; (Potential).
FT   TRANSMEM    118    138       Helical; (Potential).
FT   TRANSMEM    140    160       Helical; (Potential).
SQ   SEQUENCE   196 AA;  22711 MW;  E160131FD04D426A CRC64;
     MIIFTATLII ILAYFLGSIS GSILICKTLH FKDPRQHGSK NPGTTNILRI INYKIAIFVL
     LFDSLKGAVP IWLGTYFHID PIYLYIIAIS ACIGHIYPIY FQFYGGKGVA TAFGALTAIS
     INFFIIIIIT WILTVYLFRY ASLGSIVTFI VITFYVWYIQ YHHFEYIILL SLIILSQHKN
     NIKRLWNHQE KHIWNR
//
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