ID   PLSX_MORMI              Reviewed;         337 AA.
AC   Q9RA35;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 2.
DT   25-MAY-2022, entry version 70.
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};
OS   Moritella marina (Vibrio marinus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=90736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15381 / BCRC 15891 / CIP 102861 / NCIMB 1144 / MP-1;
RA   Morita N., Ueno A., Tanaka M., Ohgiya S., Hoshino T., Kawasaki K.,
RA   Yumoto I., Ishizaki K., Okuyama H.;
RT   "Cloning and sequencing of clustered genes involved in fatty acid
RT   biosynthesis from the docosahexaenoic acid-producing bacterium, Vibrio
RT   marinus strain MP-1.";
RL   Biotechnol. Lett. 21:641-646(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA85254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB021978; BAA85254.1; ALT_INIT; Genomic_DNA.
DR   PIR; T44432; T44432.
DR   AlphaFoldDB; Q9RA35; -.
DR   SMR; Q9RA35; -.
DR   UniPathway; UPA00085; -.
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..337
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189963"
SQ   SEQUENCE   337 AA;  36063 MW;  82B37D16144B6CBF CRC64;
     MPNLTIALDA MGGDFGPHVT IPAAINILKK YKYLSIYLVG NEAEINSLLQ NTSTSIKSRF
     TIIPSLDDIP MDLAPALALR NFKQSSMRMA LNLVREGKAQ ACVSAGNTGA LMVLSRHLLK
     VLPFVDRPAL VSTLPSMTTQ PVYMLDLGVN VSCDADALLQ FALMGSALAE HVGNIPIPRV
     ALLNVGQEDI KGNDLVKHAA QLLSKNPNLN YIGFIEGNDI FSGKADVIVC DGFTGNVALK
     TSEGVVDLVI SQLTSVSNNN IFTKLLSLLV KPLIMSSLKR LKPDQYNGAT LLGLPGIVIK
     SHGNAKQVAF EFAIEQAVKE VESGLVNKIS ASLDIID