ID   PLSX_HELMI              Reviewed;         335 AA.
AC   B0TGV6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Helmi_20920;
GN   ORFNames=HM1_2161;
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/jb.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(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; CP000930; ABZ84717.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0TGV6; -.
DR   SMR; B0TGV6; -.
DR   STRING; 498761.HM1_2161; -.
DR   EnsemblBacteria; ABZ84717; ABZ84717; HM1_2161.
DR   KEGG; hmo:HM1_2161; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_1_9; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000008550; 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; Reference proteome; Transferase.
FT   CHAIN           1..335
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000089911"
SQ   SEQUENCE   335 AA;  35104 MW;  FB7010ED82A4FF36 CRC64;
     MRIALDAMGG DHAPGEIVKG AIEAAEELHL QILLVGRPDA IEPLLKEASA GARSRLDIVA
     ASEVIAMDES PATALRKKKD ASIVVATRLV KEGRAQALVS AGSTGAQMAA SLLGLGRISG
     IDRPAIATIL PTLEGGKLLL DVGANSEAKP RNLLQFAHMG SIYAEKVMGI ANPRVALLNI
     GEEETKGNEL VLGAYGMLRE APLHFIGNVE GRDIFFGRAD VIVCDGFVGN VVLKFGEGMV
     SALKTMIKDE LKNSRMAQLG ALLAAPALRG MGKRLDYAEY GGAPLLGVNG VSIICHGSSK
     AKAIKNALRV ARQGVQQNFI AAIQEHIPGK VEPVC