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UGTP_BACC2
ID   UGTP_BACC2              Reviewed;         388 AA.
AC   B7IW03;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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};
GN   OrderedLocusNames=BCG9842_B4809;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK95619.1; -; Genomic_DNA.
DR   RefSeq; WP_000594686.1; NC_011772.1.
DR   AlphaFoldDB; B7IW03; -.
DR   SMR; B7IW03; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; ACK95619; ACK95619; BCG9842_B4809.
DR   KEGG; bcg:BCG9842_B4809; -.
DR   HOGENOM; CLU_028367_0_1_9; -.
DR   OMA; NIPYMLT; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000006744; 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_1000140341"
SQ   SEQUENCE   388 AA;  43736 MW;  E2F6FAEB4E75AF25 CRC64;
     MIKNPKVLIL TAHYGNGHVQ VAKTLEQTFR QKGIEDVIVC DLFGESHPFI TDITKYLYLK
     SYTIGKELYR LFYYGVEKIY DKKIASWYAN FGRKRLKTLL QVEKPDIVIN TFPIIAVPEL
     KKQTGISIPV YNVLTDFCVH KIWIHREVDR YFVATDHVKE LMVDIGVPAE QIVETGIPIR
     SSFELKVNPD IIYNKYQLCK NKKILLIVAG AHGVLGNVKE LCQSFMSVPN LQVVVVCGKN
     EALKQDLLSL QNQNSDALKV FGYVENIDEL FRVTSCMITK PGGITLSEAA ALQVPVILYK
     PVPGQENENA MYFEKKGAAV VIRDDSEVFA KTEALLQDDV KLLQMKEAMK SIYLPEPAGH
     IVDAILAENH AEPRHIPIKS PALAQSFT
 
 
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