ID A0A372M8U6_9ACTN Unreviewed; 479 AA.
AC A0A372M8U6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN ORFNames=DY218_07475 {ECO:0000313|EMBL:RFU87362.1};
OS Streptomyces triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU87362.1, ECO:0000313|Proteomes:UP000263094};
RN [1] {ECO:0000313|EMBL:RFU87362.1, ECO:0000313|Proteomes:UP000263094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU87362.1,
RC ECO:0000313|Proteomes:UP000263094};
RA Han C.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from
RT wheat.";
RL Submitted (AUG-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU87362.1}.
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DR EMBL; QUAK01000037; RFU87362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372M8U6; -.
DR OrthoDB; 2369748at2; -.
DR Proteomes; UP000263094; 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 Transferase {ECO:0000313|EMBL:RFU87362.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..233
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 331..448
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 51248 MW; C9B6509A1C9C1971 CRC64;
MRSDPLETAA AAAAATGTTD AAAKAPPARA GGALPARAPV PLRGDGPPVL DVVIPVYNEE
KDLAACVRRL HSHLAENFPY GRDDRDTRSG THGRCGFRIT VADNASTDRT PRIAAALARE
LTGVTSYRLD RKGRGRALRT VWSQSDAPVL AYMDVDLSTD LNALLPLVAP LISGHSDLAI
GSRLARTSRV VRGPRREFIS RAYNLILRGS LQARFSDAQC GFKAIRRDVA QRLLPMVEDT
GWFFDTELLV LAERAGLRIH EVPVDWVDDP DSTVHVVRTA AEDLKGVWRV GRALAVGALP
LDRLARPFGD DPRDRRIEGV PGGLARQLVG FCVVGALSTL FYLALYSLFR TGLGPQFANA
GALLVSAVAN TAANRRLTFG VRGRERAVRH QAQGLVVFAI GLALTSGSLA ALDAAGGGAS
HTTELTVLIA ANLAATVLRF LLLRAWVFPD RGAARPPVPE LAPTHPDTTH PGTTPRTDR
//
