ID   PLSX_MARMM              Reviewed;         351 AA.
AC   Q0APH1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Mmar10_1524;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000449; ABI65816.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0APH1; -.
DR   SMR; Q0APH1; -.
DR   STRING; 394221.Mmar10_1524; -.
DR   EnsemblBacteria; ABI65816; ABI65816; Mmar10_1524.
DR   KEGG; mmr:Mmar10_1524; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_0_5; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001964; 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; Reference proteome; Transferase.
FT   CHAIN           1..351
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_1000001785"
SQ   SEQUENCE   351 AA;  36839 MW;  7EA00414A24D99C7 CRC64;
     MTAIPTISVD AMGGDLGPAA VVEGIGHALK RWPDRKATYL LHGDEALLAP LLARHPKVAA
     VCELRHTETL VQMTDKPSEA VRRARGSSMW NAIQSVKSGE AGAIVSSGNT GALMAIGKVI
     LRMKKGVHRP AISANWPTPK GHTVVLDVGA NVQCNATQLV EFAIMGEAYH RAVFGGEAPS
     VGLLNVGQEE LKGNDTVREA DQLIRKANLD IAYQGFIEGN DISAGGIDVV VTDGFTGNIA
     LKTAEGTARL VAGWVRDALT SSLLAKLAAG LLSLGALERL RQRMDPRYIN GGVLLGLKGI
     VVKSHGGADG EGFASALGLA YVMAQSDFMA QIRANLDKFA SFEEQEVAAA S