ID A4X6T4_SALTO Unreviewed; 410 AA.
AC A4X6T4;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN OrderedLocusNames=Strop_2133 {ECO:0000313|EMBL:ABP54584.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP54584.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC Evidence={ECO:0000256|ARBA:ARBA00034053};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; CP000667; ABP54584.1; -; Genomic_DNA.
DR RefSeq; WP_011906014.1; NC_009380.1.
DR AlphaFoldDB; A4X6T4; -.
DR STRING; 369723.Strop_2133; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; stp:Strop_2133; -.
DR PATRIC; fig|369723.5.peg.2189; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_033536_3_0_11; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd04188; DPG_synthase; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR007267; GtrA_DPMS_TM.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10859:SF91; DOLICHYL-PHOSPHATE BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10859; GLYCOSYL TRANSFERASE; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF04138; GtrA; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000235};
KW Transferase {ECO:0000313|EMBL:ABP54584.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..189
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 287..402
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
SQ SEQUENCE 410 AA; 43668 MW; 258A90B64B0EF35D CRC64;
MIDTTEARAA GWSPSAGQAP VLDVVIPVYN EETDLGPCVR RLHTHLREHV PYPFRITIAD
NASVDGTLDV ARSLATDLAG VEVLHLEAKG RGRALRAAWS ASPAPVLVYM DVDLSTDLAA
LLPLVAPLIS GHSDLAIGTR LARASRVVRG AKREVISRGY NLLLRGALAA RFSDAQCGFK
AIRADVAARL LPLVRDTGWF FDTELLVLAQ RAGLRIHEVP VDWVDDPDSR VDVLATALAD
LRGIGRLGRA LVTGSLPLRQ LREQVGRAPL VPPPARVPAG LPRQLARFAV VGVASTVAYL
LLYVSVRGVL GAQPANLLAL LITAVANTAA NRRLTFGVTG RRHAGRHHLQ GLVAFGLGLA
LTSGSLALLH AVVVAPARVV ELVVLVAANL AATVLRFVLL RYAMHHRRGG
//
