UGTP_STAA8
ID UGTP_STAA8 Reviewed; 391 AA.
AC Q2FZP7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=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}; Synonyms=ypfP;
GN OrderedLocusNames=SAOUHSC_00953;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, ROLE IN GLYCOLIPID AND LTA BIOSYNTHESIS, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=RN4220;
RX PubMed=11344159; DOI=10.1128/jb.183.11.3506-3514.2001;
RA Kiriukhin M.Y., Debabov D.V., Shinabarger D.L., Neuhaus F.C.;
RT "Biosynthesis of the glycolipid anchor in lipoteichoic acid of
RT Staphylococcus aureus RN4220: role of YpfP, the diglucosyldiacylglycerol
RT synthase.";
RL J. Bacteriol. 183:3506-3514(2001).
RN [3]
RP PATHWAY, AND ROLE IN GLYCOLIPID AND LTA BIOSYNTHESIS.
RC STRAIN=RN4220;
RX PubMed=17209021; DOI=10.1128/jb.01683-06;
RA Gruendling A., Schneewind O.;
RT "Genes required for glycolipid synthesis and lipoteichoic acid anchoring in
RT Staphylococcus aureus.";
RL J. Bacteriol. 189:2521-2530(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 two glucosyl residues to diacylglycerol
CC (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-
CC (beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-diglucosyl-DAG
CC (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-
CC sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found
CC in Bacillales and is also used as a membrane anchor for lipoteichoic
CC acid (LTA). UgtP can only use UDP-glucose as sugar donor.
CC {ECO:0000255|HAMAP-Rule:MF_01280, ECO:0000269|PubMed:11344159,
CC ECO:0000269|PubMed:17209021}.
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 Evidence={ECO:0000269|PubMed:11344159};
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 ECO:0000269|PubMed:11344159};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for UDP-glucose (at 15 degrees Celsius)
CC {ECO:0000269|PubMed:11344159};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11344159};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01280, ECO:0000269|PubMed:17209021}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01280,
CC ECO:0000269|PubMed:11344159}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are defective in beta-
CC diglucosyl-DAG and are smaller than wild-type. Diacylglycerol (DAG) is
CC the anchor of the LTA in the mutant. {ECO:0000269|PubMed:11344159}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. UgtP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01280}.
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DR EMBL; CP000253; ABD30078.1; -; Genomic_DNA.
DR RefSeq; WP_000258650.1; NZ_LS483365.1.
DR RefSeq; YP_499506.1; NC_007795.1.
DR AlphaFoldDB; Q2FZP7; -.
DR SMR; Q2FZP7; -.
DR STRING; 1280.SAXN108_1014; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR EnsemblBacteria; ABD30078; ABD30078; SAOUHSC_00953.
DR GeneID; 3920664; -.
DR KEGG; sao:SAOUHSC_00953; -.
DR PATRIC; fig|93061.5.peg.875; -.
DR eggNOG; COG0707; Bacteria.
DR HOGENOM; CLU_028367_0_1_9; -.
DR OMA; NIPYMLT; -.
DR BioCyc; MetaCyc:MON-20002; -.
DR UniPathway; UPA00894; -.
DR PRO; PR:Q2FZP7; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047228; F:1,2-diacylglycerol 3-glucosyltransferase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Glycosyltransferase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase.
FT CHAIN 1..391
FT /note="Processive diacylglycerol beta-glucosyltransferase"
FT /id="PRO_0000308444"
SQ SEQUENCE 391 AA; 44548 MW; A1D6E96C91B7E99D CRC64;
MVTQNKKILI ITGSFGNGHM QVTQSIVNQL NDMNLDHLSV IEHDLFMEAH PILTSICKKW
YINSFKYFRN MYKGFYYSRP DKLDKCFYKY YGLNKLINLL IKEKPDLILL TFPTPVMSVL
TEQFNINIPV ATVMTDYRLH KNWITPYSTR YYVATKETKQ DFIDVGIDPS TVKVTGIPID
NKFETPINQK QWLIDNNLDP DKQTILMSAG AFGVSKGFDT MITDILAKSA NAQVVMICGK
SKELKRSLTA KFKSNENVLI LGYTKHMNEW MASSQLMITK PGGITITEGF ARCIPMIFLN
PAPGQELENA LYFEEKGFGK IADTPEEAIK IVASLTNGNE QLTNMISTME QDKIKYATQT
ICRDLLDLIG HSSQPQEIYG KVPLYARFFV K
