UGTP_STAAC
ID UGTP_STAAC Reviewed; 391 AA.
AC Q5HH69; O86492;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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}; OrderedLocusNames=SACOL1022;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9650993; DOI=10.1089/mdr.1998.4.85;
RA Ludovice A.M., Wu S.-W., de Lencastre H.;
RT "Molecular cloning and DNA sequencing of the Staphylococcus aureus UDP-N-
RT acetylmuramyl tripeptide synthetase (murE) gene, essential for the optimal
RT expression of methicillin resistance.";
RL Microb. Drug Resist. 4:85-90(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PROCESSIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=10848996; DOI=10.1046/j.1432-1327.2000.01414.x;
RA Jorasch P., Warnecke D.C., Lindner B., Zaehringer U., Heinz E.;
RT "Novel processive and nonprocessive glycosyltransferases from
RT Staphylococcus aureus and Arabidopsis thaliana synthesize
RT glycoglycerolipids, glycophospholipids, glycosphingolipids and
RT glycosylsterols.";
RL Eur. J. Biochem. 267:3770-3783(2000).
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). In vitro, UgtP can also use cholesterol,
CC cholesterolglucoside and the fluorescent substrate 6-(N-7-nitrobenz-2-
CC oxa-1,3-diazol-4-yl)-amino-caproyl-sphingosine (NBD-ceramide) as sugar
CC acceptors, but it can only use UDP-glucose as sugar donor.
CC {ECO:0000255|HAMAP-Rule:MF_01280, ECO:0000269|PubMed:10848996}.
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:10848996};
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:10848996};
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; Y14370; CAA74741.1; -; Genomic_DNA.
DR EMBL; CP000046; AAW36488.1; -; Genomic_DNA.
DR RefSeq; WP_000258650.1; NC_002951.2.
DR AlphaFoldDB; Q5HH69; -.
DR SMR; Q5HH69; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR EnsemblBacteria; AAW36488; AAW36488; SACOL1022.
DR KEGG; sac:SACOL1022; -.
DR HOGENOM; CLU_028367_0_1_9; -.
DR OMA; NIPYMLT; -.
DR BRENDA; 2.4.1.315; 3352.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000000530; 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; Transferase.
FT CHAIN 1..391
FT /note="Processive diacylglycerol beta-glucosyltransferase"
FT /id="PRO_0000308445"
FT CONFLICT 254..258
FT /note="SNENV -> LTRMY (in Ref. 1; CAA74741)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="L -> F (in Ref. 1; CAA74741)"
FT /evidence="ECO:0000305"
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
