ID   PLSX_PROMM              Reviewed;         448 AA.
AC   Q7V4F7;
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=PMT_1995;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
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; BX548175; CAE22169.1; -; Genomic_DNA.
DR   RefSeq; WP_011131360.1; NC_005071.1.
DR   AlphaFoldDB; Q7V4F7; -.
DR   SMR; Q7V4F7; -.
DR   STRING; 74547.PMT_1995; -.
DR   EnsemblBacteria; CAE22169; CAE22169; PMT_1995.
DR   KEGG; pmt:PMT_1995; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_0_0_3; -.
DR   OMA; HGKSNAR; -.
DR   OrthoDB; 631784at2; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001423; 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..448
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189920"
FT   REGION          1..105
FT                   /note="Unknown"
FT   REGION          106..448
FT                   /note="Phosphate acyltransferase"
SQ   SEQUENCE   448 AA;  47353 MW;  80A15024922CD96E CRC64;
     MPPKDSDSST ASGPRSKTTR PRAIRRLVIW YRRNAAVTSL VGSATNSASA AGNVAGTVVS
     SAGSVVSNAG SMAGSMLQPL VFDPLRRLQS SENNPEAEDI KNSDRLWVAV DGMGGDEAPG
     PILDGCLKAI QRLPLRIKFV GETEKVLGAV QAMGLTELFN QATAAGHLEL VASGPSVGMD
     EEATVVRRKR DASINLTMDL VKKGEALAMY SAGNSGAMMA SAIFRLGRLA GIDRPAIGAL
     FPTKDPTQPV LVLDVGANMD CKPIYLHQFA LLGNIYSRDV LQVARPRIGL LNIGEEECKG
     NDLAIRTHEL LSEEHRLQFA GNCEGRDVLS GAFDVVVCDG FTGNVLLKFL ESVGSVLLDV
     LRAELPRGRR GKVGSAFLRS NLKRIKKRLD HAEHGGALLL GVNGICVIGH GSSKALSVVS
     ALRLAHSAAS HGVMDDLAEL QKAPVESA