ID   PLSX_ENDTX              Reviewed;         338 AA.
AC   B1H0Q6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE            EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019};
DE   AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019};
DE   AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE   AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
GN   Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; OrderedLocusNames=TGRD_605;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
CC   -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl-
CC       PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme
CC       utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC       {ECO:0000255|HAMAP-Rule:MF_00019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-
CC         [ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:138651; EC=2.3.1.274; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00019};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   -!- SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00019}.
CC       Note=Associated with the membrane possibly through PlsY.
CC       {ECO:0000255|HAMAP-Rule:MF_00019}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
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DR   EMBL; AP009510; BAG14088.1; -; Genomic_DNA.
DR   RefSeq; WP_015423612.1; NC_020419.1.
DR   RefSeq; YP_001956549.1; NC_020419.1.
DR   AlphaFoldDB; B1H0Q6; -.
DR   SMR; B1H0Q6; -.
DR   STRING; 471821.TGRD_605; -.
DR   EnsemblBacteria; BAG14088; BAG14088; TGRD_605.
DR   KEGG; rsd:TGRD_605; -.
DR   PATRIC; fig|471821.5.peg.994; -.
DR   HOGENOM; CLU_039379_1_1_0; -.
DR   OMA; HGKSNAR; -.
DR   OrthoDB; 631784at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001691; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00019; PlsX; 1.
DR   InterPro; IPR003664; FA_synthesis.
DR   InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR   PANTHER; PTHR30100; PTHR30100; 1.
DR   Pfam; PF02504; FA_synthesis; 1.
DR   PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR   TIGRFAMs; TIGR00182; plsX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..338
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000089947"
SQ   SEQUENCE   338 AA;  36289 MW;  0FC6576901A80FA0 CRC64;
     MIIALDAMGG DFAPASTVEG AIFAAKESKH KILLVGIEKI LVGELLKYRG RYDLKSLNIE
     IINATEFITM DEHPAKAVRQ KKDSSLSVCA RLVADGKADA FVSMGNSGAA MSAALFYLKR
     IEGVLRPAIS TVFPNFGGHC IIADMGANVD CTPEYLLQFG IMASLFCEKV ASVENPRVGL
     VSIGEESTKG NELTLAAFEL LKKADINFIG NVEGRDIPGG KVDVAICDGF VGNVILKLGE
     GLTEMMLKLI RKEFKQHPMT WASLPFLWLA IKDLRKRVDY SEFGGAPLLG VEGVCIIGHG
     SSNGKAVKNA IFAGAETAKH NIAAGIKEAI LRYNNKVV