PLSY_BACSU
ID PLSY_BACSU Reviewed; 193 AA.
AC Q45064;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glycerol-3-phosphate acyltransferase;
DE AltName: Full=Acyl-PO4 G3P acyltransferase;
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase;
DE AltName: Full=G3P acyltransferase;
DE Short=GPAT;
DE EC=2.3.1.275;
DE AltName: Full=Lysophosphatidic acid synthase;
DE Short=LPA synthase;
GN Name=plsY; Synonyms=yneS; OrderedLocusNames=BSU18070;
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=8969507; DOI=10.1099/13500872-142-11-3097;
RA Rose M., Entian K.-D.;
RT "New genes in the 170 degrees region of the Bacillus subtilis genome encode
RT DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid
RT transporter.";
RL Microbiology 142:3097-3101(1996).
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 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 [4]
RP FUNCTION, AND ACTIVITY REGULATION.
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 [5]
RP FUNCTION, AND 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).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate
CC (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic
CC acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor,
CC but not acyl-CoA or acyl-ACP. {ECO:0000269|PubMed:17557823,
CC ECO:0000269|PubMed:17645809, ECO:0000269|PubMed:19282621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:59918; EC=2.3.1.275;
CC -!- ACTIVITY REGULATION: Inhibited by acyl-CoA.
CC {ECO:0000269|PubMed:17557823}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000269|PubMed:19282621}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000305}.
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DR EMBL; Z73234; CAA97604.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13690.1; -; Genomic_DNA.
DR PIR; A69892; A69892.
DR RefSeq; NP_389689.1; NC_000964.3.
DR RefSeq; WP_003231560.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q45064; -.
DR SMR; Q45064; -.
DR STRING; 224308.BSU18070; -.
DR TCDB; 9.B.31.1.2; the plsy/yqih (plsy) family.
DR PaxDb; Q45064; -.
DR PRIDE; Q45064; -.
DR EnsemblBacteria; CAB13690; CAB13690; BSU_18070.
DR GeneID; 938037; -.
DR KEGG; bsu:BSU18070; -.
DR PATRIC; fig|224308.179.peg.1969; -.
DR eggNOG; COG0344; Bacteria.
DR InParanoid; Q45064; -.
DR OMA; WRHRGNL; -.
DR PhylomeDB; Q45064; -.
DR BioCyc; BSUB:BSU18070-MON; -.
DR BRENDA; 2.3.1.275; 658.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
DR TIGRFAMs; TIGR00023; TIGR00023; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..193
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188326"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 193 AA; 20966 MW; C75803C399B97292 CRC64;
MLIALLIILA YLIGSIPSGL IVGKLAKGID IREHGSGNLG ATNAFRTLGV KAGSVVIAGD
ILKGTLATAL PFLMHVDIHP LLAGVFAVLG HVFPIFAKFK GGKAVATSGG VLLFYAPLLF
ITMVAVFFIF LYLTKFVSLS SMLTGIYTVI YSFFVHDTYL LIVVTLLTIF VIYRHRANIK
RIINKTEPKV KWL
