PLSX_ENTFA
ID PLSX_ENTFA Reviewed; 333 AA.
AC Q82ZE8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=EF_3112;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS), AND SUBUNIT.
RX PubMed=19058030; DOI=10.1007/s10969-008-9052-9;
RA Kim Y., Li H., Binkowski T.A., Holzle D., Joachimiak A.;
RT "Crystal structure of fatty acid/phospholipid synthesis protein PlsX from
RT Enterococcus faecalis.";
RL J. Struct. Funct. Genomics 10:157-163(2009).
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, ECO:0000269|PubMed:19058030}.
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; AE016830; AAO82792.1; -; Genomic_DNA.
DR RefSeq; NP_816722.1; NC_004668.1.
DR RefSeq; WP_002387382.1; NZ_KE136524.1.
DR PDB; 1U7N; X-ray; 2.26 A; A/B=1-333.
DR PDBsum; 1U7N; -.
DR AlphaFoldDB; Q82ZE8; -.
DR SMR; Q82ZE8; -.
DR STRING; 226185.EF_3112; -.
DR EnsemblBacteria; AAO82792; AAO82792; EF_3112.
DR KEGG; efa:EF3112; -.
DR PATRIC; fig|226185.45.peg.461; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_1_9; -.
DR OMA; HGKSNAR; -.
DR BRENDA; 2.3.1.274; 2095.
DR UniPathway; UPA00085; -.
DR EvolutionaryTrace; Q82ZE8; -.
DR Proteomes; UP000001415; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..333
FT /note="Phosphate acyltransferase"
FT /id="PRO_0000189878"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1U7N"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 226..251
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1U7N"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:1U7N"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:1U7N"
SQ SEQUENCE 333 AA; 35835 MW; 1BA33F81B65A47E8 CRC64;
MKIAVDAMGG DNAPQAIVEG VMLAKQDFPD IEFQLYGKEA EIKKYITDEK NITIIHTDEK
IASDDEPVKA IRRKKTASMV LAAQAVKNGE ADAIFSAGNT GALLAAGLFI VGRIKNVERP
GLMSTLPVMG EPDKGFDMLD LGANADNKPE HLVQYAVLGS FYAEKVRNVQ NPRVGLLNNG
TEETKGSELT KKAFELLAAD ETINFVGNVE ARELLNGVAD VVVTDGFTGN AVLKSIEGTA
MNMMSLLKTA ILSEGVKGKM GALLLKNALH GMKDEMDYSK HGGAVLFGLK APVIKTHGAT
GPDAVRYTIR QIHTMLETQV VPQLVEYYEG KAE
