ID   PLSX_PROMA              Reviewed;         436 AA.
AC   Q7VE56;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Phosphate acyltransferase;
DE            EC=2.3.1.274;
DE   AltName: Full=Acyl-ACP phosphotransacylase;
DE   AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase;
DE   AltName: Full=Phosphate-acyl-ACP acyltransferase;
GN   Name=plsX; OrderedLocusNames=Pro_0157;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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 (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC   -!- SUBUNIT: Homodimer. Probably interacts with PlsY (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with the
CC       membrane possibly through PlsY. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000305}.
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DR   EMBL; AE017126; AAP99203.1; -; Genomic_DNA.
DR   RefSeq; NP_874551.1; NC_005042.1.
DR   RefSeq; WP_011124312.1; NC_005042.1.
DR   AlphaFoldDB; Q7VE56; -.
DR   SMR; Q7VE56; -.
DR   STRING; 167539.Pro_0157; -.
DR   EnsemblBacteria; AAP99203; AAP99203; Pro_0157.
DR   GeneID; 54199516; -.
DR   KEGG; pma:Pro_0157; -.
DR   PATRIC; fig|167539.5.peg.163; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_0_0_3; -.
DR   OMA; HGKSNAR; -.
DR   OrthoDB; 631784at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001420; 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   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..436
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189919"
SQ   SEQUENCE   436 AA;  46220 MW;  63B9425EF5ED1CC3 CRC64;
     MDNESRSKAI RPKAIRRLVI WYRRNSAVTT LVDTATNSAS AAGNVAGSVV SSAGSVVSSA
     GSIARSTLQP LVFDPLRRLQ AGPNELDRND IANSKRLWVA VDGMGGDNAP GSILEGCLQA
     IDRLPLCIKF VGEIEKIHSA ADELGISDLL NQLISAGNIE LVASGPSIGM DEEATAVRKK
     RDASINIAMD LVKKGEALSV YSAGNSGALM AAAIFRLGRL AGIDRPAIGA LFPTKDPGQP
     VLVLDVGANM DCKPAYLHQF ALLGNIYSRD VLQVQNPRIG LLNIGEEECK GNDLSLRTFE
     LLKEEERLDF VGNCEGRDVL SGDFDVVVCD GFTGNVLLKF LESVGSVLLD VLRAELPRGR
     RGKVGSAFLR NNLKRIKKRL DHAEHGGALL LGVNGICVIG HGSSKALSVV SALRIAHSAA
     SHGVMDDLAA LQPPQP