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Database: UniProt
Entry: A0A1G5INE5_9ACTN
LinkDB: A0A1G5INE5_9ACTN
Original site: A0A1G5INE5_9ACTN 
ID   A0A1G5INE5_9ACTN        Unreviewed;       424 AA.
AC   A0A1G5INE5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE            EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN   ORFNames=SAMN02745898_103442 {ECO:0000313|EMBL:SCY77109.1};
OS   Streptomyces sp. 136MFCol5.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCY77109.1, ECO:0000313|Proteomes:UP000199326};
RN   [1] {ECO:0000313|EMBL:SCY77109.1, ECO:0000313|Proteomes:UP000199326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCY77109.1,
RC   ECO:0000313|Proteomes:UP000199326};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FMVI01000003; SCY77109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5INE5; -.
DR   Proteomes; UP000199326; Unassembled WGS sequence.
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:UP000199326};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..188
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          286..403
FT                   /note="GtrA/DPMS transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04138"
SQ   SEQUENCE   424 AA;  45641 MW;  94860AA135A3C508 CRC64;
     MPAREHLLAG AVDAADAPVL DVVVPVYNEE KDLETCVLRL HDHLVRTFPY AFRITVADNA
     STDRTPQVAA RLAAFLPRCR SYRLEEKGRG RALRTVWSQS DAPVLAYMDV DLSTDLNALL
     PLVAPLISGH SDLAIGSRLA RSSRVVRGSK REFISRAYNL ILRSSLAARF SDAQCGFKAI
     RRDVAQRLLP MVEDTGWFFD TEMLVLAERA GLRIHEVPVD WVDDPDSTVH IVRTATEDLK
     GVWRVGRALA VGALPLDRLA RPFGDDPRDR GLSGVPGGLA RQLVGFCVVG ALSTLFYLAL
     YSLFRLGAGP QIANGGALLV SAVANTAANR RLTFGVRGRS GAVRHQAQGL VVFAVGLALT
     SGSLAALGAA SGSPSHGTEL AVLIAANLAA TVLRFLLLRA WVFPDRAPAT GRADDTHHEL
     GNVR
//
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