UGTP_BACAN
ID UGTP_BACAN Reviewed; 388 AA.
AC Q81YW9; Q6I3R7; Q6KXI2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
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};
GN OrderedLocusNames=BA_0511, GBAA_0511, BAS0483;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(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}.
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DR EMBL; AE016879; AAP24533.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29605.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52814.1; -; Genomic_DNA.
DR RefSeq; NP_843047.1; NC_003997.3.
DR RefSeq; WP_000594708.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_026763.1; NC_005945.1.
DR AlphaFoldDB; Q81YW9; -.
DR SMR; Q81YW9; -.
DR STRING; 261594.GBAA_0511; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR DNASU; 1087727; -.
DR EnsemblBacteria; AAP24533; AAP24533; BA_0511.
DR EnsemblBacteria; AAT29605; AAT29605; GBAA_0511.
DR GeneID; 45020560; -.
DR KEGG; ban:BA_0511; -.
DR KEGG; bar:GBAA_0511; -.
DR KEGG; bat:BAS0483; -.
DR PATRIC; fig|198094.11.peg.510; -.
DR eggNOG; COG0707; Bacteria.
DR HOGENOM; CLU_028367_0_1_9; -.
DR OMA; NIPYMLT; -.
DR UniPathway; UPA00894; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..388
FT /note="Processive diacylglycerol beta-glucosyltransferase"
FT /id="PRO_0000308447"
SQ SEQUENCE 388 AA; 43761 MW; 258505FF5A850662 CRC64;
MIKNPKVLIL TAHYGNGHVQ VAKTLEQTFR QKGIKDVIVC DLFGESHPVI TDITKYLYLK
SYTIGKELYR LFYYGVEKIY DKKIASWYAN FGRKRLKLLL QAEKPDIVIN TFPIIAVPEL
KKQTGISIPV YNVLTDFCVH KIWIHREVDR YFVATDHVKK VMVDIGVPAE QIVETGIPIR
SSFELKINPD IIYNKYQLCK NKKILLIVAG AHGVLGSVKE LCQSFMSVPD LQVVVVCGKN
EALKQDLVGV QETNPDALKV FGYVENIDEL FRVTSCMITK PGGITLSEAA ALQVPVILYK
PVPGQENENA MYFERKGAAV VIRDDSEVFA KTEALLQDDM KLLQMKEAMK SIYRPEPADH
IVDTILAENH VEPNHIPIKS PALAQSFT
