ID   PLSX_WOLTR              Reviewed;         345 AA.
AC   Q5GS21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=Wbm0615;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(2005).
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; AE017321; AAW71203.1; -; Genomic_DNA.
DR   RefSeq; WP_011256813.1; NC_006833.1.
DR   AlphaFoldDB; Q5GS21; -.
DR   SMR; Q5GS21; -.
DR   STRING; 292805.Wbm0615; -.
DR   EnsemblBacteria; AAW71203; AAW71203; Wbm0615.
DR   KEGG; wbm:Wbm0615; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_0_5; -.
DR   OMA; HGKSNAR; -.
DR   OrthoDB; 631784at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000534; 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..345
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000001860"
SQ   SEQUENCE   345 AA;  37358 MW;  0B93E5724AB0BC81 CRC64;
     MLPTVNNNIV IALDAMGGDF APLSVIQGAG FFLDNLVDPG IKVFFHIYGD QKEISPLLLK
     YRKVSDNSEF THYSNNVLAN DKPSFALRHR KDSSMKAAIE AVKKGKASGM VSSGNTGALM
     AISRFILGTL PNVYRPAIVS VCPTKAKSFA LLDLGANVDC NVDSLFQFAL MGSMFAKIAL
     KVDNPEVALL NIGTEEVKGN DSVRGAFKLL KSAPNINFKG YIEASEFLEG NIDVIVADGF
     VGNVMLKTAE ATASTFIDLI KQEMFNSWAT KMLVGILLKS KLNKVLMRFN PKIRSGAMFL
     GLNGIVIKSH GNSDAVSFAH AIKFAVNSIN ENLNQKIISE VNQVE