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UGTP_BACC1
ID   UGTP_BACC1              Reviewed;         388 AA.
AC   Q73DZ5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Beta-triglucosyldiacylglycerol synthase {ECO:0000255|HAMAP-Rule:MF_01280};
DE            Short=TGlcDAG 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=BCE_0565;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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 up to three glucosyl residues to
CC       diacylglycerol (DAG), thereby catalyzing the formation of beta-
CC       monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol),
CC       beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-
CC       glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O-
CC       (beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D-
CC       glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the
CC       predominant glycolipid found in Bacillales and is also used as a
CC       membrane anchor for lipoteichoic acid (LTA). {ECO:0000255|HAMAP-
CC       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-3-O-(beta-D-Glc-(1->6)-beta-D-Glc)-sn-glycerol +
CC         UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-Glc-(1->6)-beta-D-Glc-
CC         (1->6)-beta-D-Glc)-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:39027,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:76264, ChEBI:CHEBI:76265; 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}.
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DR   EMBL; AE017194; AAS39500.1; -; Genomic_DNA.
DR   RefSeq; WP_000594712.1; NC_003909.8.
DR   AlphaFoldDB; Q73DZ5; -.
DR   SMR; Q73DZ5; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; AAS39500; AAS39500; BCE_0565.
DR   GeneID; 59159089; -.
DR   KEGG; bca:BCE_0565; -.
DR   HOGENOM; CLU_028367_0_1_9; -.
DR   OMA; NIPYMLT; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000002527; Chromosome.
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..388
FT                   /note="Processive diacylglycerol beta-glucosyltransferase"
FT                   /id="PRO_0000308448"
SQ   SEQUENCE   388 AA;  43806 MW;  0BC97AF17B18DA54 CRC64;
     MIKNPKVLIL TAHYGNGHVQ VAKTLEQTFR QKGIKDVIVC DLFGESHPVI TDITKYLYLK
     SYTIGKELYR LFYYGVEKIY DKKIASWYAN FGRKRLKLLL QAEKPDIVIN TFPIIAVPEL
     KKQTGISIPV YNVLTDFCVH KIWIHREVDR YFVATDHVKK VMVDIGVPAE QIVETGIPIR
     SSFELKINSD IIYNKYQLCK NKKILLIVAG AHGVLGSVKE LCQSFMSVPD LQVVVVCGKN
     EALKQDLLGL QEKNPDALKV FGYVENIDEL FRVTSCMITK PGGITLSEAA ALQVPVILYK
     PVPGQENENA MYFERKGAAV VIRDDSEVFA KTEALLQDDM KLLQMKEAMK SIYRPEPADH
     IVDTILAENH VEPNHIPIKS PALAQSFT
 
 
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