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UGTP_STACT
ID   UGTP_STACT              Reviewed;         391 AA.
AC   B9DQ98;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Sca_0619;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(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 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). {ECO:0000255|HAMAP-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-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; AM295250; CAL27533.1; -; Genomic_DNA.
DR   RefSeq; WP_015899876.1; NC_012121.1.
DR   AlphaFoldDB; B9DQ98; -.
DR   SMR; B9DQ98; -.
DR   STRING; 396513.SCA_0619; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   GeneID; 60545682; -.
DR   KEGG; sca:SCA_0619; -.
DR   eggNOG; COG0707; Bacteria.
DR   HOGENOM; CLU_028367_0_1_9; -.
DR   OMA; HSYWIHP; -.
DR   OrthoDB; 1165736at2; -.
DR   BioCyc; SCAR396513:SCA_RS03150-MON; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000000444; 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..391
FT                   /note="Processive diacylglycerol beta-glucosyltransferase"
FT                   /id="PRO_1000165235"
SQ   SEQUENCE   391 AA;  45153 MW;  E8791136429A8FCE CRC64;
     MVTQNKKILI ITGSFGNGHL QVTNSVVNQL NEMNLKHLSV IEHDLFMEAH PILTSICKKY
     YINSFKYFRN SYKQFYYSRP EDVNKCFYKY YGLNKLINLL IKEKPDLILL TFPTPVMSVL
     TEQFNMNIPI ATVMTDYRLH KNWVTPHSSR YYVATPDLKQ EFVNVGVPED IIKITGIPIS
     EQFDEDIDTK VWMHKNHLDP NRPTILMSAG AFGVSKGFDV MISDILERSP ETQIVMICGR
     NKELKRALRQ QFKEYANVLI LGYTHHMNEW MASSHLMVTK PGGITISEAL ARKIPMIFLD
     PAPGQELENA HYFQSKGMGK IADTTEEAIQ LITELTQDEN ALAHMAEQMQ DLKVKYPTYK
     LCRDLLHLLD HSSQFEEIYG KVPMYAKLFI K
 
 
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