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Database: UniProt
Entry: A0A1G9C9W1_9ACTN
LinkDB: A0A1G9C9W1_9ACTN
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ID   A0A1G9C9W1_9ACTN        Unreviewed;       418 AA.
AC   A0A1G9C9W1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE            EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN   ORFNames=SAMN05421869_116115 {ECO:0000313|EMBL:SDK48440.1};
OS   Nonomuraea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=633440 {ECO:0000313|EMBL:SDK48440.1, ECO:0000313|Proteomes:UP000199202};
RN   [1] {ECO:0000313|EMBL:SDK48440.1, ECO:0000313|Proteomes:UP000199202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDK48440.1,
RC   ECO:0000313|Proteomes:UP000199202};
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; FNDJ01000016; SDK48440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9C9W1; -.
DR   STRING; 633440.SAMN05421869_116115; -.
DR   OrthoDB; 2369748at2; -.
DR   Proteomes; UP000199202; 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:UP000199202};
KW   Transferase {ECO:0000313|EMBL:SDK48440.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        382..404
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          285..403
FT                   /note="GtrA/DPMS transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04138"
SQ   SEQUENCE   418 AA;  44692 MW;  89DF83D4D1DB1C48 CRC64;
     MSTSASSASV TAPRLPANAP VLDVVVPVHN EQDDLEPCVR RLRHHLVNEF PYTFRITIAD
     NASTDRTHQI AVGLAAELPE VSYVRLAAKG RGRALKHAWS ASDSPVLAYM DVDLSTDLAA
     LLPLVAPLIS GHSELAIGSR LTRGARVTRG PKREIISRCY NLLLRGTLSA RFSDAQCGFK
     AVRADVAARL LPLVQDTGWF FDTELLVLTE RAGLRIHEVP VDWVDDPDSR VDILRTAVAD
     LKGIARLVTA LGTGRLALSS LREQLGRSPR PVPGVPAGLT GQLLRFAAVG IVSTLAYLLL
     YALLRTQTGA QTANLVALLV TAVANTALNR RFAFGVRGTG RLWLHQAQGL LVFAVSLGLT
     GGSLALLQAL APAPAAPLEL GVLVAANLAT TCLRFLLLRT WVFGGVPSAV ARRRPPRS
//
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