ID   PLSX_PROMP              Reviewed;         466 AA.
AC   Q7V3E1;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=PMM0135;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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; BX548174; CAE18594.1; -; Genomic_DNA.
DR   RefSeq; WP_011131774.1; NC_005072.1.
DR   AlphaFoldDB; Q7V3E1; -.
DR   SMR; Q7V3E1; -.
DR   STRING; 59919.PMM0135; -.
DR   EnsemblBacteria; CAE18594; CAE18594; PMM0135.
DR   KEGG; pmm:PMM0135; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_0_0_3; -.
DR   OMA; HGKSNAR; -.
DR   OrthoDB; 631784at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001026; 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; Transferase.
FT   CHAIN           1..466
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189921"
FT   REGION          1..122
FT                   /note="Unknown"
FT   REGION          123..466
FT                   /note="Phosphate acyltransferase"
SQ   SEQUENCE   466 AA;  49856 MW;  1604CFE47F385BE2 CRC64;
     MEKDSSIKKS RAIRRLVIWY KRNSAVTSIV DTAANSAVTA SNVAGNVVSG AGSVVSTASN
     VAGNVAGNVV SSAESVVNTA SNVVSSASSI AKNTLQPLVF DPLKRLQNSD NLISKEEVPN
     SERIWIAVDG MGGDYAPVPI LEGCLGAISR FPINIKFVGK IEKVRYEAER VGLIDLLEKE
     IDNNRLELID SGDPIGMNEE ATAVRKRKDA SINVAMDLVK TNKAKAVYSA GNSGALMASA
     IFRIGRLKGI ERPAIGALFP TRDQTRPVLV LDVGANTDCK PSYLHQFALL GNVYAKDVLQ
     IEKPRIGLLN IGEEECKGND LSIKTFELLS NEKSFNFGGN CEGRDVLSGD FDVVVCDGFT
     GNILLKFLES VGGVLLDILR SELPRGRRGK VGSAFLKSNL LRIKKRLDHA EHGGALLLGV
     NGICVIGHGS SKSLSVVSAL RLAHSAVNHN VMENLNQLQK LQVLNS