PLSY_STRR6
ID PLSY_STRR6 Reviewed; 213 AA.
AC P0A4Q0; Q54916;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 {ECO:0000269|PubMed:16949372};
DE AltName: Full=Lysophosphatidic acid synthase;
DE Short=LPA synthase;
GN Name=plsY; OrderedLocusNames=spr0755;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND NOMENCLATURE.
RX PubMed=16949372; DOI=10.1016/j.molcel.2006.06.030;
RA Lu Y.-J., Zhang Y.-M., Grimes K.D., Qi J., Lee R.E., Rock C.O.;
RT "Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive
RT pathogens.";
RL Mol. Cell 23:765-772(2006).
RN [3]
RP TOPOLOGY, MUTAGENESIS OF SER-36; ASN-43; ARG-46; GLY-102; GLY-103; LYS-104;
RP HIS-185 AND ASN-188, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17308305; DOI=10.1074/jbc.m700374200;
RA Lu Y.-J., Zhang F., Grimes K.D., Lee R.E., Rock C.O.;
RT "Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-
RT phosphate acyltransferase.";
RL J. Biol. Chem. 282:11339-11346(2007).
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:16949372}.
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 Evidence={ECO:0000269|PubMed:16949372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl phosphate + sn-glycerol 3-phosphate = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + phosphate;
CC Xref=Rhea:RHEA:54968, ChEBI:CHEBI:43474, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:138436;
CC Evidence={ECO:0000269|PubMed:16949372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54969;
CC Evidence={ECO:0000269|PubMed:16949372};
CC -!- ACTIVITY REGULATION: Inhibited by acyl-CoA and 1-acylglycerol-3-
CC phosphate. {ECO:0000269|PubMed:16949372, ECO:0000269|PubMed:17308305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for glycerol-3-phosphate (at 37 degrees Celsius and at pH
CC 7.4) {ECO:0000269|PubMed:17308305};
CC KM=30 uM for acyl-phosphate (at 37 degrees Celsius and at pH 7.4)
CC {ECO:0000269|PubMed:17308305};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:17308305};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000305}.
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DR EMBL; AE007317; AAK99559.1; -; Genomic_DNA.
DR PIR; C97966; C97966.
DR RefSeq; NP_358349.1; NC_003098.1.
DR RefSeq; WP_000628789.1; NC_003098.1.
DR AlphaFoldDB; P0A4Q0; -.
DR SMR; P0A4Q0; -.
DR STRING; 171101.spr0755; -.
DR SwissLipids; SLP:000001798; -.
DR EnsemblBacteria; AAK99559; AAK99559; spr0755.
DR GeneID; 60233452; -.
DR KEGG; spr:spr0755; -.
DR PATRIC; fig|171101.6.peg.835; -.
DR eggNOG; COG0344; Bacteria.
DR HOGENOM; CLU_081254_4_0_9; -.
DR OMA; WRHRGNL; -.
DR BioCyc; MetaCyc:MON-14087; -.
DR BRENDA; 2.3.1.275; 1960.
DR SABIO-RK; P0A4Q0; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000000586; 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..213
FT /note="Glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000188465"
FT TOPO_DOM 1..3
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 36
FT /note="S->A: Loss of acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 43
FT /note="N->A: 5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 46
FT /note="R->A: Loss of acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 102
FT /note="G->A: Defect in substrate binding."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 103
FT /note="G->A: Defect in substrate binding."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 104
FT /note="K->A: Loss of acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 185
FT /note="H->A: 0.6% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:17308305"
FT MUTAGEN 188
FT /note="N->A: Loss of acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17308305"
SQ SEQUENCE 213 AA; 22929 MW; 22CB089C17750818 CRC64;
MITIVLLILA YLLGSIPSGL WIGQVFFQIN LREHGSGNTG TTNTFRILGK KAGMATFVID
FFKGTLATLL PIIFHLQGVS PLIFGLLAVI GHTFPIFAGF KGGKAVATSA GVIFGFAPIF
CLYLAIIFFG ALYLGSMISL SSVTASIAAV IGVLLFPLFG FILSNYDSLF IAIILALASL
IIIRHKDNIA RIKNKTENLV PWGLNLTHQD PKK
