UGTP_BACCQ
ID UGTP_BACCQ Reviewed; 388 AA.
AC B9J2U2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=BCQ_0539;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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}.
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; CP000227; ACM11011.1; -; Genomic_DNA.
DR RefSeq; WP_000594713.1; NC_011969.1.
DR AlphaFoldDB; B9J2U2; -.
DR SMR; B9J2U2; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR EnsemblBacteria; ACM11011; ACM11011; BCQ_0539.
DR KEGG; bcq:BCQ_0539; -.
DR HOGENOM; CLU_028367_0_1_9; -.
DR OMA; NIPYMLT; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000000441; 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_1000165234"
SQ SEQUENCE 388 AA; 43834 MW; B67FB2017B18DA4A 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 RLLQMKEAMK SIYRPEPADH
IVDTILAENH VEPNHIPIKS PALAQSFT
