ID   PLSX_MARN8              Reviewed;         340 AA.
AC   A1U1T2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Maqu_1869;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1U1T2; -.
DR   SMR; A1U1T2; -.
DR   STRING; 351348.Maqu_1869; -.
DR   EnsemblBacteria; ABM18951; ABM18951; Maqu_1869.
DR   KEGG; maq:Maqu_1869; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_0_6; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000998; 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; Transferase.
FT   CHAIN           1..340
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000329239"
SQ   SEQUENCE   340 AA;  36760 MW;  DC10ACD23195A315 CRC64;
     MPHGRVVNTP VTIAIDAMSG DRGAAVVVHA ALEAVRENEA LSLVLVGIRS ELEALLHEGH
     ARIRIVEAAD VVRMNERPSH ALRHKKNSSM AIALSLVRDG EAQGCVSAGN TGALMAFGRS
     IIRMYPGIER PAIAKLIPSL RGRCHVLDLG ANVDSTAENL YQYALMGSLM ASAICRQSEP
     RVALLNVGEE EIKGNEQVRL ASHMLAQCDT INYIGYVEGS DLFRDVADVV VCDGFVGNIA
     LKTGEGVAGL LIELLEQAFT RSMYGRFVGL LARPIIGRLL QLMDPSRHNG ASLLGLQGVV
     IKSHGNANER AMLAAIRQAV REVQLEVPRR INERLDDLML