ID A0A1T5CZN3_9MICC Unreviewed; 477 AA.
AC A0A1T5CZN3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN ORFNames=SAMN05660473_01740 {ECO:0000313|EMBL:SKB64837.1};
OS Arthrobacter sp. 49Tsu3.1M3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1279029 {ECO:0000313|EMBL:SKB64837.1, ECO:0000313|Proteomes:UP000189904};
RN [1] {ECO:0000313|EMBL:SKB64837.1, ECO:0000313|Proteomes:UP000189904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=49Tsu3.1M3 {ECO:0000313|EMBL:SKB64837.1,
RC ECO:0000313|Proteomes:UP000189904};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUZD01000005; SKB64837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5CZN3; -.
DR Proteomes; UP000189904; 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:SKB64837.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..232
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 333..452
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 50686 MW; 291FBCCC0AA9F164 CRC64;
MTFTDQATGT LPRSTATPAG PAAPESSSGL ALADAPVPGP IAGALTGPSG RRTAIDTRAS
TPLLDVTIPV FNEERDLEAC LRRLHAYLLG AFPHSFRITV ADNASTDGTL KAAERVAREL
REVTVVHMAE KGRGNALRRV WLASPSPVLA YMDVDLSTDL AALGPLLAPL ISGHSDLAIG
TRLTRNSRVV RGPKREFISR SYNFLLQALM GAHFSDAQCG FKAIRADVAR QLLPHTLDNA
WFFDTELLVL AEKCGLRVHE VPVDWTDDPD SSVDIVQTAL ADLRGMARLS RDLVSGRIPV
PDLRAALARG PLPAASRAQE QSPGESLFGQ LVRFGSIGVA STLAYLAIFL LCRGFMDPQL
ANFLALLTTA VANTAANRRF TFGIQGSSQA ARHHFEGLLV FGIGLALTSG ALALVHAVSG
AAPDRWLELL TVTAANLAAT AVKFLLFRLV VFRHRPAAAV PASGAPGPSL PRTEKAK
//
