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Processive diacylglycerol beta-glucosyltransferase (EC 2.4.1.315) (Beta-diglucosyldiacylglycerol synthase) (Beta-DGS) (DGlcDAG synthase) (Glc2-DAG synthase) (Beta-gentiobiosyldiacylglycerol synthase) (Beta-monoglucosyldiacylglycerol synthase) (Beta-MGS) (MGlcDAG synthase) (Beta-triglucosyldiacylglycerol synthase) (TGlcDAG synthase) (Diglucosyl diacylglycerol synthase (1,6-linking)) (Glucosyl-beta-1,6-glucosyldiacylglycerol synthase) (UDP glucosyltransferase) (UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase)

 J8AND8_BACCE            Unreviewed;       388 AA.
J8AND8;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
20-DEC-2017, entry version 28.
RecName: Full=Processive diacylglycerol beta-glucosyltransferase {ECO:0000256|HAMAP-Rule:MF_01280};
EC=2.4.1.315 {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=Beta-diglucosyldiacylglycerol synthase {ECO:0000256|HAMAP-Rule:MF_01280};
Short=Beta-DGS {ECO:0000256|HAMAP-Rule:MF_01280};
Short=DGlcDAG synthase {ECO:0000256|HAMAP-Rule:MF_01280};
Short=Glc2-DAG synthase {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=Beta-gentiobiosyldiacylglycerol synthase {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=Beta-monoglucosyldiacylglycerol synthase {ECO:0000256|HAMAP-Rule:MF_01280};
Short=Beta-MGS {ECO:0000256|HAMAP-Rule:MF_01280};
Short=MGlcDAG synthase {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=Beta-triglucosyldiacylglycerol synthase {ECO:0000256|HAMAP-Rule:MF_01280};
Short=TGlcDAG synthase {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=Diglucosyl diacylglycerol synthase (1,6-linking) {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=Glucosyl-beta-1,6-glucosyldiacylglycerol synthase {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=UDP glucosyltransferase {ECO:0000256|HAMAP-Rule:MF_01280};
AltName: Full=UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase {ECO:0000256|HAMAP-Rule:MF_01280};
Name=ugtP {ECO:0000256|HAMAP-Rule:MF_01280};
ORFNames=IEE_04679 {ECO:0000313|EMBL:EJQ40990.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ40990.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ40990.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ40990.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Processive glucosyltransferase involved in the
biosynthesis of both the bilayer- and non-bilayer-forming membrane
glucolipids. Is able to successively transfer up to three glucosyl
residues to diacylglycerol (DAG), thereby catalyzing the formation
of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-
sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-
beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-
triglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-
glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-
glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found
in Bacillales and is also used as a membrane anchor for
lipoteichoic acid (LTA). {ECO:0000256|HAMAP-Rule:MF_01280}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + 1,2-diacyl-3-O-(beta-D-
glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-(beta-D-
glucopyranosyl-(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol + UDP.
{ECO:0000256|HAMAP-Rule:MF_01280}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + 1,2-diacyl-3-O-(beta-D-
glucopyranosyl-(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol = 1,2-
diacyl-3-O-(beta-D-glucopyranosyl-(1->6)-beta-D-glucopyranosyl-
(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol + UDP.
{ECO:0000256|HAMAP-Rule:MF_01280}.
-!- CATALYTIC ACTIVITY: UDP-glucose + 1,2-diacyl-sn-glycerol = UDP +
1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol.
{ECO:0000256|HAMAP-Rule:MF_01280}.
-!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01280}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01280}.
-!- SIMILARITY: Belongs to the glycosyltransferase 28 family. UgtP
subfamily. {ECO:0000256|HAMAP-Rule:MF_01280}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJQ40990.1}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AHDJ01000042; EJQ40990.1; -; Genomic_DNA.
RefSeq; WP_002201852.1; NZ_JH791996.1.
EnsemblBacteria; EJQ40990; EJQ40990; IEE_04679.
PATRIC; fig|1053189.3.peg.4780; -.
UniPathway; UPA00894; -.
Proteomes; UP000006600; Unassembled WGS sequence.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0047228; F:1,2-diacylglycerol 3-glucosyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009247; P:glycolipid biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_01280; Diacylglyc_glucosyltr; 1.
InterPro; IPR009695; Diacylglyc_glucosyltr_N.
InterPro; IPR007235; Glyco_trans_28_C.
InterPro; IPR023589; Pro_diacylglycrl_glcsylTrfase.
Pfam; PF04101; Glyco_tran_28_C; 1.
Pfam; PF06925; MGDG_synth; 1.
3: Inferred from homology;
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01280};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01280};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006600};
Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01280};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01280};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01280};
Membrane {ECO:0000256|HAMAP-Rule:MF_01280};
Transferase {ECO:0000256|HAMAP-Rule:MF_01280}.
DOMAIN 18 179 MGDG_synth. {ECO:0000259|Pfam:PF06925}.
DOMAIN 224 348 Glyco_tran_28_C.
{ECO:0000259|Pfam:PF04101}.
COILED 240 260 {ECO:0000256|SAM:Coils}.
SEQUENCE 388 AA; 43707 MW; 4F9F29A28FA6A34D CRC64;
MIKNPKVLIL TAHYGNGHVQ VAKTLEQTFH QKGIKDVIVC DLFGESHPVI TDITKYLYLK
SYTVGKELYR LFYYGVEKIY DKKIASWYAN FGRKRLKTLL QVEKPDIVIN TFPIIAVPEL
KKQIGISIPV YNVLTDFCVH KIWIHREVDR YFVATDHVKK VMVDIGVPAE QIVETGIPIR
SSFELKINPA IIYNKYQLCK DKKMLLIVAG AHGVLGSVKE LCQSFMSVPN LQVVVVCGKN
EALKQDLMEL QEQSSDALKV FGYVENIDEL FRVTSCMITK PGGITLSEAA ALQVPVILYK
PVPGQENENA LYFEKKGAAV VIRDDSEVFA KTEALLQDDM KLLQMKEAMK SIYRPEPAGH
IVDTILAENH AEPNHIPIKS PALAESFT


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