ID   PLSX_MYCPN              Reviewed;         328 AA.
AC   P75232;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 120.
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};
GN   OrderedLocusNames=MPN_546; ORFNames=MP296;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95944.1; -; Genomic_DNA.
DR   PIR; S73622; S73622.
DR   RefSeq; WP_010874903.1; NC_000912.1.
DR   AlphaFoldDB; P75232; -.
DR   SMR; P75232; -.
DR   STRING; 272634.MPN_546; -.
DR   PaxDb; 272634-MPN_546; -.
DR   EnsemblBacteria; AAB95944; AAB95944; MPN_546.
DR   KEGG; mpn:MPN_546; -.
DR   PATRIC; fig|272634.6.peg.608; -.
DR   HOGENOM; CLU_039379_1_1_14; -.
DR   OrthoDB; 9806408at2; -.
DR   BioCyc; MPNE272634:G1GJ3-900-MONOMER; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000000808; 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:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_00019; PlsX; 1.
DR   InterPro; IPR003664; FA_synthesis.
DR   InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR   NCBIfam; TIGR00182; plsX; 1.
DR   PANTHER; PTHR30100; FATTY ACID/PHOSPHOLIPID SYNTHESIS PROTEIN PLSX; 1.
DR   PANTHER; PTHR30100:SF1; PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF02504; FA_synthesis; 1.
DR   PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..328
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189909"
SQ   SEQUENCE   328 AA;  36664 MW;  2BACE0DD9ADE32E7 CRC64;
     MAFRLAVDCL GFENHPREAI DAVLEYWSYH QELEFILVGD EKTFDGLDYL PKNITKQLAS
     SCIDMTDTPL TARRKVNNSM QKAINLVRDG AADVVISAGS SAVYASLTYD GFGKIHKDVK
     SAFMSYVPTA NNDWFYFLDV GANKNFTGKE LYFLGLMADI FVKKTTNKIS PRIALLNIGT
     EIHKGFDYHQ EGYQLLNEDK HLNFTGFIEP RFLLDGVCDI LVADGYSGNL VLKSMEGTFK
     TIARLLKQGY KRNPLAGLFS LGILKRIAKR FDYKNNAGAV VIGLNKLALK THGSADKQQF
     LSTIRLAHTS LKSDLINAIK SSLDNYEK
//