ID   PLSX_SALTY              Reviewed;         359 AA.
AC   P0A259; O85138;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=STM1192;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=9642179; DOI=10.1128/jb.180.13.3295-3303.1998;
RA   Zhang Y., Cronan J.E. Jr.;
RT   "Transcriptional analysis of essential genes of the Escherichia coli fatty
RT   acid biosynthesis gene cluster by functional replacement with the analogous
RT   Salmonella typhimurium gene cluster.";
RL   J. Bacteriol. 180:3295-3303(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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=AAC38647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF044668; AAC38647.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE006468; AAL20121.1; -; Genomic_DNA.
DR   RefSeq; NP_460162.1; NC_003197.2.
DR   RefSeq; WP_001518286.1; NC_003197.2.
DR   AlphaFoldDB; P0A259; -.
DR   SMR; P0A259; -.
DR   STRING; 99287.STM1192; -.
DR   PaxDb; P0A259; -.
DR   EnsemblBacteria; AAL20121; AAL20121; STM1192.
DR   GeneID; 1252710; -.
DR   KEGG; stm:STM1192; -.
DR   PATRIC; fig|99287.12.peg.1261; -.
DR   HOGENOM; CLU_039379_1_0_6; -.
DR   OMA; HGKSNAR; -.
DR   PhylomeDB; P0A259; -.
DR   BioCyc; SENT99287:STM1192-MON; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001014; 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..359
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189931"
SQ   SEQUENCE   359 AA;  38716 MW;  ADD01BA971D5ECD8 CRC64;
     MTRLTLALDV MGGDFGPSVT VPAALQALNA NSQLTLLLVG NPDIITPLLA KADFEQRSRL
     QIIPAQSVIA SDARPSQAIR ASRGTSMRVA LELVKEGRAE ACVSAGNTGA LMGLAKLLLK
     PLEGIERPAL VTVLPHQQKG KTVVLDLGAN VDCDSTMLVQ FAVMGAVLAE EVVGIKNPRV
     ALLNIGEEET KGLDSIREAS LMLKTVPTIN YIGYLEANEL LTGKTDVLVC DGFTGNVTLK
     TMEGVVRMFL SLLKSQGEGK KRSWWLLLLK RWLQKSLTRR FSHLNPDQYN GACLLGLRGT
     VIKSHGAANQ RAFAVAIEQA VQAVQRQVPQ RIAARLESVY PAGFEPLDDG KGVNLRAHR