UGTP_BACP2
ID UGTP_BACP2 Reviewed; 383 AA.
AC A8FED1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, 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=BPUM_1928;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(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 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; CP000813; ABV62598.1; -; Genomic_DNA.
DR RefSeq; WP_012010316.1; NZ_VEIS01000001.1.
DR AlphaFoldDB; A8FED1; -.
DR SMR; A8FED1; -.
DR STRING; 315750.BPUM_1928; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR PRIDE; A8FED1; -.
DR EnsemblBacteria; ABV62598; ABV62598; BPUM_1928.
DR KEGG; bpu:BPUM_1928; -.
DR eggNOG; COG0707; Bacteria.
DR HOGENOM; CLU_028367_0_1_9; -.
DR OMA; NIPYMLT; -.
DR OrthoDB; 1165736at2; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000001355; 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; IPR001296; Glyco_trans_1.
DR InterPro; IPR023589; Pro_diacylglycrl_glcsylTrfase.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF06925; MGDG_synth; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Glycosyltransferase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase.
FT CHAIN 1..383
FT /note="Processive diacylglycerol beta-glucosyltransferase"
FT /id="PRO_1000067410"
SQ SEQUENCE 383 AA; 43680 MW; 2DD85F41BACE9D98 CRC64;
MNTNKKILIL TANYGNGHMQ VAKTLYDECK SQGFEHVVVS NLYQESNPIV SEVTQYLYLK
SFSIGKQFYR LFYYGVDKIY NKRKFNIYLK MGNKRLDELI QLHNPDIIII TFPMIVVPEY
RNKTGKIIPT FNVMTDFCLH KIWVHENIDR YYVATDYVKQ KLVEIGTHPS DVKVTGIPIR
PQFEADVPKS KIYKKYGLSS NKKVLLIMAG AHGVLKNVKE LCEALLLDSE VQIVVVCGKN
AALKQSLSDL EQTHPDQLKA LGYVEQIDEL FRVTDCMITK PGGITLTEAT ALGVPVILYK
PVPGQEKENA HFFEDYGAAI VINRHEDILE SVTNLLQDEE KLESMKQNMK SLHLKHSSQT
ILEDIVEQSD LITNNKTYAR ALS
