ID   UGTP_STAAE              Reviewed;         391 AA.
AC   A6QFM7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=Processive diacylglycerol beta-glucosyltransferase {ECO:0000255|HAMAP-Rule:MF_01280};
DE            EC=2.4.1.315;
DE   AltName: Full=Beta-diglucosyldiacylglycerol synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE            Short=Beta-DGS {ECO:0000255|HAMAP-Rule:MF_01280};
DE            Short=DGlcDAG synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE            Short=Glc2-DAG synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE   AltName: Full=Beta-gentiobiosyldiacylglycerol synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE   AltName: Full=Beta-monoglucosyldiacylglycerol synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE            Short=Beta-MGS {ECO:0000255|HAMAP-Rule:MF_01280};
DE            Short=MGlcDAG synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE   AltName: Full=Diglucosyl diacylglycerol synthase (1,6-linking);
DE   AltName: Full=Glucosyl-beta-1,6-glucosyldiacylglycerol synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE   AltName: Full=UDP glucosyltransferase {ECO:0000255|HAMAP-Rule:MF_01280};
DE   AltName: Full=UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase {ECO:0000255|HAMAP-Rule:MF_01280};
GN   Name=ugtP {ECO:0000255|HAMAP-Rule:MF_01280};
GN   OrderedLocusNames=NWMN_0887;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
CC   -!- FUNCTION: Processive glucosyltransferase involved in the biosynthesis
CC       of both the bilayer- and non-bilayer-forming membrane glucolipids. Is
CC       able to successively transfer two glucosyl residues to diacylglycerol
CC       (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-
CC       (beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-diglucosyl-DAG
CC       (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-
CC       sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found
CC       in Bacillales and is also used as a membrane anchor for lipoteichoic
CC       acid (LTA). {ECO:0000255|HAMAP-Rule:MF_01280}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + UDP-
CC         alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc)-sn-
CC         glycerol + UDP + H(+); Xref=Rhea:RHEA:39031, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75799,
CC         ChEBI:CHEBI:76264; EC=2.4.1.315;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-
CC         3-O-(beta-D-glucopyranosyl)-sn-glycerol + UDP + H(+);
CC         Xref=Rhea:RHEA:17285, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75799;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01280};
CC   -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01280}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01280}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. UgtP
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01280}.
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DR   EMBL; AP009351; BAF67159.1; -; Genomic_DNA.
DR   RefSeq; WP_000258650.1; NC_009641.1.
DR   AlphaFoldDB; A6QFM7; -.
DR   SMR; A6QFM7; -.
DR   KEGG; sae:NWMN_0887; -.
DR   HOGENOM; CLU_028367_0_1_9; -.
DR   UniPathway; UPA00894; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047228; F:1,2-diacylglycerol 3-glucosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd17507; GT28_Beta-DGS-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   HAMAP; MF_01280; Diacylglyc_glucosyltr; 1.
DR   InterPro; IPR009695; Diacylglyc_glucosyltr_N.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   InterPro; IPR050519; Glycosyltransf_28_UgtP.
DR   InterPro; IPR023589; Pro_diacylglycrl_glcsylTrfase.
DR   NCBIfam; NF010134; PRK13608.1; 1.
DR   PANTHER; PTHR43025; MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE; 1.
DR   PANTHER; PTHR43025:SF3; MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF06925; MGDG_synth; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Glycosyltransferase;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Transferase.
FT   CHAIN           1..391
FT                   /note="Processive diacylglycerol beta-glucosyltransferase"
FT                   /id="PRO_1000073185"
SQ   SEQUENCE   391 AA;  44548 MW;  A1D6E96C91B7E99D CRC64;
     MVTQNKKILI ITGSFGNGHM QVTQSIVNQL NDMNLDHLSV IEHDLFMEAH PILTSICKKW
     YINSFKYFRN MYKGFYYSRP DKLDKCFYKY YGLNKLINLL IKEKPDLILL TFPTPVMSVL
     TEQFNINIPV ATVMTDYRLH KNWITPYSTR YYVATKETKQ DFIDVGIDPS TVKVTGIPID
     NKFETPINQK QWLIDNNLDP DKQTILMSAG AFGVSKGFDT MITDILAKSA NAQVVMICGK
     SKELKRSLTA KFKSNENVLI LGYTKHMNEW MASSQLMITK PGGITITEGF ARCIPMIFLN
     PAPGQELENA LYFEEKGFGK IADTPEEAIK IVASLTNGNE QLTNMISTME QDKIKYATQT
     ICRDLLDLIG HSSQPQEIYG KVPLYARFFV K
//