ID   PLSX_RHOCA              Reviewed;         399 AA.
AC   P30789;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 78.
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};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1961742; DOI=10.1073/pnas.88.23.10749;
RA   Toussaint B., Bosc C., Richaud P., Colbeau A., Vignais P.M.;
RT   "A mutation in a Rhodobacter capsulatus gene encoding an integration host
RT   factor-like protein impairs in vivo hydrogenase expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10749-10753(1991).
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; M84030; AAA26126.1; -; Genomic_DNA.
DR   PIR; B41608; B41608.
DR   AlphaFoldDB; P30789; -.
DR   SMR; P30789; -.
DR   UniPathway; UPA00085; -.
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..399
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189928"
SQ   SEQUENCE   399 AA;  41052 MW;  AF8641E794E3F64E CRC64;
     MVKLFKQETT TVGVEADVTS SRGCPAAAQA PDVSGALISG VPVSAPLVLS IDAMGGDRGP
     AAVLDGIALA RRKYPDLHFL VHGPEADVAP LVKARRLKSC VTIRHATGVV TMHDKPAAVM
     RGGKDTSMWS TIDAVRDGAA QVAVSCGNTG ALMAVSMLRL RKMPGVNRPA IAAFWPCKNP
     SGFNIMLDMG ADVKAEARDL LTYALMGSSY ARNALGLDRP RVGLLNVGTE EHKGHAELKI
     AAEMIGAMET AGGYEFVGFV EGNDLPGSRV DVIVTDGFTG NVALKTGEGT AKFAGELMRE
     AFTSSLLSKL GALLASGALK RLKAKIDPRR VNGGVFLGLN GTVIKSHGGA DATGVAAAID
     LAARLAGLGF AERLAARVAL ASANGQDAAS AEAGIENAK