ID   PLSX_ECOLI              Reviewed;         356 AA.
AC   P27247;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   04-NOV-2026, entry version 157.
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=b1090, JW5156;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1447160; DOI=10.1128/jb.174.23.7873-7874.1992;
RA   Oh W., Larson T.J.;
RT   "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the
RT   Escherichia coli K-12 chromosome.";
RL   J. Bacteriol. 174:7873-7874(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-30.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [5]
RP   FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=17645809; DOI=10.1186/1471-2180-7-69;
RA   Yoshimura M., Oshima T., Ogasawara N.;
RT   "Involvement of the YneS/YgiH and PlsX proteins in phospholipid
RT   biosynthesis in both Bacillus subtilis and Escherichia coli.";
RL   BMC Microbiol. 7:69-69(2007).
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, ECO:0000269|PubMed:17645809}.
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. Note=Associated with the membrane
CC       possibly through PlsY. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB59064.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M96793; AAB59064.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC74174.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35898.2; -; Genomic_DNA.
DR   PIR; G64852; G64852.
DR   RefSeq; NP_415608.2; NC_000913.3.
DR   RefSeq; WP_000197597.1; NZ_CP009789.1.
DR   AlphaFoldDB; P27247; -.
DR   SMR; P27247; -.
DR   BioGRID; 4261030; 152.
DR   DIP; DIP-10517N; -.
DR   FunCoup; P27247; 458.
DR   IntAct; P27247; 1.
DR   STRING; 511145.b1090; -.
DR   jPOST; P27247; -.
DR   PaxDb; 511145-b1090; -.
DR   EnsemblBacteria; AAC74174; AAC74174; b1090.
DR   GeneID; 946165; -.
DR   KEGG; ecj:JW5156; -.
DR   KEGG; eco:b1090; -.
DR   PATRIC; fig|511145.12.peg.1133; -.
DR   EchoBASE; EB1407; -.
DR   eggNOG; COG0416; Bacteria.
DR   HOGENOM; CLU_039379_1_0_6; -.
DR   InParanoid; P27247; -.
DR   OMA; AAADLMX; -.
DR   OrthoDB; 9806408at2; -.
DR   PhylomeDB; P27247; -.
DR   BioCyc; EcoCyc:EG11437-MONOMER; -.
DR   UniPathway; UPA00085; -.
DR   PRO; PR:P27247; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P27247; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IMP:EcoCyc.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0055088; P:lipid homeostasis; IMP:EcoCyc.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IGI:EcoCyc.
DR   GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:EcoCyc.
DR   FunFam; 3.40.718.10:FF:000008; Phosphate acyltransferase; 1.
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   1: Evidence at protein level;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..356
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189875"
SQ   SEQUENCE   356 AA;  38214 MW;  89C6C64C57184DF4 CRC64;
     MTRLTLALDV MGGDFGPSVT VPAALQALNS NSQLTLLLVG NSDAITPLLA KADFEQRSRL
     QIIPAQSVIA SDARPSQAIR ASRGSSMRVA LELVKEGRAQ ACVSAGNTGA LMGLAKLLLK
     PLEGIERPAL VTVLPHQQKG KTVVLDLGAN VDCDSTMLVQ FAIMGSVLAE EVVEIPNPRV
     ALLNIGEEEV KGLDSIRDAS AVLKTIPSIN YIGYLEANEL LTGKTDVLVC DGFTGNVTLK
     TMEGVVRMFL SLLKSQGEGK KRSWWLLLLK RWLQKSLTRR FSHLNPDQYN GACLLGLRGT
     VIKSHGAANQ RAFAVAIEQA VQAVQRQVPQ RIAARLESVY PAGFELLDGG KSGTLR
//