ID   PLSX_UREPA              Reviewed;         331 AA.
AC   Q9PQT7;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, 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=UU206;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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; AF222894; AAF30613.1; -; Genomic_DNA.
DR   RefSeq; WP_006688948.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQT7; -.
DR   SMR; Q9PQT7; -.
DR   STRING; 273119.UU206; -.
DR   EnsemblBacteria; AAF30613; AAF30613; UU206.
DR   GeneID; 29672706; -.
DR   KEGG; uur:UU206; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_1_14; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000423; 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..331
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189960"
SQ   SEQUENCE   331 AA;  37118 MW;  830E4DDF9C747CF1 CRC64;
     MEKIKILLDT MGYENDLEHV IKAAKDFYYQ HEDDLEIILV GNEQLIKPLL DNDWRLFPIV
     HTEVSIEQND TILSARKKQN SSMHLALRYL KDKQADGMLT AGNSAVFVYN AYATIGLLEH
     IKKPAFMPFV PTIDGGVTNL LDVGASIDVD GTDLFNFAIM ANTIAKMRTP NPRVGVLNIG
     TEDHKGLPYH QEANELLKTS NLNYVGFVEP KTILEREVDV LVADGFSGNI ALKTMEGVGK
     TISNFLKNEY KKPKNLFAAL LSKPIFKKIK KAFDYKEHAG AFVLGLDGIL VKTHGSADYQ
     QFMSALKILY ETIKADVLNE IKKDLNNYYG Q