ID   PLSX_FRATW              Reviewed;         348 AA.
AC   A4IWY2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=FTW_0519;
OS   Francisella tularensis subsp. tularensis (strain WY96-3418).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=418136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WY96-3418;
RX   PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA   Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA   Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA   Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA   Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT   "Complete genomic characterization of a pathogenic A.II strain of
RT   Francisella tularensis subspecies tularensis.";
RL   PLoS ONE 2:E947-E947(2007).
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; CP000608; ABO46434.1; -; Genomic_DNA.
DR   RefSeq; WP_003016130.1; NC_009257.1.
DR   AlphaFoldDB; A4IWY2; -.
DR   SMR; A4IWY2; -.
DR   KEGG; ftw:FTW_0519; -.
DR   HOGENOM; CLU_039379_1_0_6; -.
DR   OMA; HGKSNAR; -.
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..348
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000001765"
SQ   SEQUENCE   348 AA;  37840 MW;  0B6AC1600AFC07DD CRC64;
     MGYKISIDAM GGDHGLNTTI PAALEAVKKD SNLQIVLVGD HHKIKRALDR YSKVKKIKLP
     VLQRIAIHHA SETVGMDESP SIAVRKKKDS SMRVAINLVK DRTVDACVSA GNTGALMATS
     KFVLKTINGV DRPAIVYALP AFNRETKQLS KTYMLDLGAN VVCTSEQLFQ FAIMGSILAA
     SSKGIAEPRV SLLNIGEEEM KGLDNIKNAA KLLQGCDFIN YNGYIEGKYI FDDTTDVIVC
     DGFVGNVSLK TMEGSLRLIE SLIKKTIQES SLLMKIPIVM ALPIFKKMKK GMNLDSFNGA
     SLLGLTGIVV KSHGGASANA FETAIYEAIK EIKYNIPKTI QESLEKVL