ID   PLSX_PSEAE              Reviewed;         336 AA.
AC   Q9HZN5;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 2.
DT   03-AUG-2022, entry version 104.
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=PA2969;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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=AAG06357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004091; AAG06357.1; ALT_INIT; Genomic_DNA.
DR   PIR; A83273; A83273.
DR   RefSeq; NP_251659.1; NC_002516.2.
DR   RefSeq; WP_071533934.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZN5; -.
DR   SMR; Q9HZN5; -.
DR   STRING; 287.DR97_4970; -.
DR   PaxDb; Q9HZN5; -.
DR   PRIDE; Q9HZN5; -.
DR   EnsemblBacteria; AAG06357; AAG06357; PA2969.
DR   GeneID; 880143; -.
DR   KEGG; pae:PA2969; -.
DR   PATRIC; fig|208964.12.peg.3115; -.
DR   PseudoCAP; PA2969; -.
DR   HOGENOM; CLU_039379_1_0_6; -.
DR   InParanoid; Q9HZN5; -.
DR   OMA; HGKSNAR; -.
DR   PhylomeDB; Q9HZN5; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000002438; 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..336
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189922"
SQ   SEQUENCE   336 AA;  35549 MW;  9BAC7FC7E9966E7A CRC64;
     MSAPIIAIDA MGGDFGPHCV VPASIAFLAE NSSSQLILVG QPALLEELLS RYPSLDRQRL
     RVHAASEVIG SDERPSQALR GKPDASMRVA LELVRDGRAH ACVSAGNTGA LMALSRHLLK
     TLPGIDRPAM VTAVPTEKGH CHLLDLGANV DCSAEHLYQF AVMGAVAAEA LGCVSPRVAL
     LNVGTEEIKG NQQVKLAASL LQKAQGLNFS GYIEGDGLYR GEADVVVCDG FVGNILLKAS
     EGLAAMVSAR IEQRFRDGLA AKLVGALALP LLRRLRGDIA PARYNGASFL GLQGIVVKSH
     GSAAEEGFQS ALRRAALEVR ENLPQRLHGR LEHLLL