PLSX_BACSU
ID PLSX_BACSU Reviewed; 333 AA.
AC P71018; O34561;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=ylpD;
GN OrderedLocusNames=BSU15890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-333.
RC STRAIN=168;
RX PubMed=8759840; DOI=10.1128/jb.178.16.4794-4800.1996;
RA Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.;
RT "Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid
RT biosynthesis genes.";
RL J. Bacteriol. 178:4794-4800(1996).
RN [4]
RP FUNCTION IN PHOSPHOLIPID BIOSYNTHESIS.
RC STRAIN=168;
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).
RN [5]
RP FUNCTION.
RX PubMed=17557823; DOI=10.1128/jb.00602-07;
RA Paoletti L., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT "Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis.";
RL J. Bacteriol. 189:5816-5824(2007).
RN [6]
RP INTERACTION.
RC STRAIN=168;
RX PubMed=19282621; DOI=10.1266/ggs.83.433;
RA Hara Y., Seki M., Matsuoka S., Hara H., Yamashita A., Matsumoto K.;
RT "Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-
RT phosphate acyltransferase PlsY in the initial stage of glycerolipid
RT synthesis in Bacillus subtilis.";
RL Genes Genet. Syst. 83:433-442(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-333, AND FUNCTION.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
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:16021622,
CC ECO:0000269|PubMed:17557823, 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 (By similarity). Probably interacts with PlsY.
CC {ECO:0000255|HAMAP-Rule:MF_00019, ECO:0000269|PubMed:19282621}.
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 ---------------------------------------------------------------------------
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; Y13937; CAA74248.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13462.1; -; Genomic_DNA.
DR EMBL; U59433; AAC44305.1; -; Genomic_DNA.
DR PIR; H69679; H69679.
DR PIR; T46631; T46631.
DR RefSeq; NP_389471.1; NC_000964.3.
DR RefSeq; WP_003232041.1; NZ_JNCM01000035.1.
DR PDB; 1VI1; X-ray; 2.95 A; A/B=2-333.
DR PDB; 6A1K; X-ray; 2.30 A; A/B=1-326.
DR PDBsum; 1VI1; -.
DR PDBsum; 6A1K; -.
DR AlphaFoldDB; P71018; -.
DR SMR; P71018; -.
DR STRING; 224308.BSU15890; -.
DR jPOST; P71018; -.
DR PaxDb; P71018; -.
DR EnsemblBacteria; CAB13462; CAB13462; BSU_15890.
DR GeneID; 938066; -.
DR KEGG; bsu:BSU15890; -.
DR PATRIC; fig|224308.179.peg.1729; -.
DR eggNOG; COG0416; Bacteria.
DR InParanoid; P71018; -.
DR OMA; HGKSNAR; -.
DR PhylomeDB; P71018; -.
DR BioCyc; BSUB:BSU15890-MON; -.
DR BRENDA; 2.3.1.274; 658.
DR UniPathway; UPA00085; -.
DR EvolutionaryTrace; P71018; -.
DR Proteomes; UP000001570; 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_0000189847"
FT CONFLICT 66..74
FT /note="DEPVRAVRR -> MNRSVPCEA (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:6A1K"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1VI1"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 225..250
FT /evidence="ECO:0007829|PDB:6A1K"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1VI1"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6A1K"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:6A1K"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:1VI1"
SQ SEQUENCE 333 AA; 35763 MW; 2FB6A2E8A034199E CRC64;
MRIAVDAMGG DHAPKAVIDG VIKGIEAFDD LHITLVGDKT TIESHLTTTS DRITVLHADE
VIEPTDEPVR AVRRKKNSSM VLMAQEVAEN RADACISAGN TGALMTAGLF IVGRIKGIDR
PALAPTLPTV SGDGFLLLDV GANVDAKPEH LVQYAIMGSV YSQQVRGVTS PRVGLLNVGT
EDKKGNELTK QTFQILKETA NINFIGNVEA RDLLDDVADV VVTDGFTGNV TLKTLEGSAL
SIFKMMRDVM TSTLTSKLAA AVLKPKLKEM KMKMEYSNYG GASLFGLKAP VIKAHGSSDS
NAVFHAIRQA REMVSQNVAA LIQEEVKEEK TDE
