ID   UGTP_STAAB              Reviewed;         391 AA.
AC   Q2YWW6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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}; OrderedLocusNames=SAB0883c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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 + H(+) + UDP; 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 + H(+) + UDP;
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}.
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; AJ938182; CAI80571.1; -; Genomic_DNA.
DR   RefSeq; WP_000258639.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWW6; -.
DR   SMR; Q2YWW6; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   KEGG; sab:SAB0883c; -.
DR   HOGENOM; CLU_028367_0_1_9; -.
DR   OMA; NIPYMLT; -.
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   HAMAP; MF_01280; Diacylglyc_glucosyltr; 1.
DR   InterPro; IPR009695; Diacylglyc_glucosyltr_N.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   InterPro; IPR023589; Pro_diacylglycrl_glcsylTrfase.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF06925; MGDG_synth; 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_0000308454"
SQ   SEQUENCE   391 AA;  44548 MW;  FDB22F2C13BFC91A CRC64;
     MVTQNKKILI ITGSFGNGHM QVTQSIVNQL NDMNLDHLSV IEHDLFMEAH PILTSICKKW
     YINSFKYFRN MYKGFYYSRP DKLDKCFYKY YGLNKLINLL IKEKPDLILL TFPTPVMSVL
     TEQFNINIPV ATVMTDYRLH KNWITPYSTR YYVATKETKK DFIDVGIDPS TVKVTGIPID
     NKFETPINQK QWLIDNNLDP DKQTILMSAG AFGVSKGFDT MITDILAKSA NAQVVMICGK
     SKELKRSLTA KFKSNENVLI LGYTKHMNEW MASSQLMITK PGGITITEGF ARCIPMIFLN
     PAPGQELENA LYFEEKGFGK IADTPEEAIK IVASLTNGNE QLTNMISTME QDKIKYATQT
     ICRDLLDLIG HSSQPQEIYG KVPLYARFFV K