ID A0A0H4BVZ2_9ACTN Unreviewed; 481 AA.
AC A0A0H4BVZ2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN ORFNames=QR97_03630 {ECO:0000313|EMBL:AKN69023.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN69023.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN69023.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN69023.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) 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; CP011799; AKN69023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4BVZ2; -.
DR STRING; 1577075.QR97_03630; -.
DR PATRIC; fig|1577075.3.peg.747; -.
DR Proteomes; UP000036399; 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:UP000036399};
KW Transferase {ECO:0000313|EMBL:AKN69023.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..192
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 292..409
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
FT REGION 416..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 52570 MW; 49F3008310CA3616 CRC64;
MRTDSSPGTL PAREHLPAGD AGTPVLDVVI PVHNEEKDLP PCVRRLHAHL TRTFPYAFRI
TIADNASTDT TPLVAARLAA EIPEVAAFRL EQKGRGRALR TVWSVSDAPV LAYMDVDLST
DLNALLPLVA PLISGHSDLA IGSRLARASR VVRGPKREFV SRAYNLILRG SLQARFSDAQ
CGFKAIRREV AQVLLPLVED TGWFFDTEML VLAERAGLRI HEVPVDWVDD PDSTVHIVQT
ATDDLKGVWR VGKALATGSL PLDRLTRPFG DDPRDRELPD VPGGLARQLL GFCAVGVLST
LFYLLLYSAF RQFTGSQTAN ALALLVSATA NTAANRRLTF GVRGRRGAVR HQAQGLVVLG
IGLALTSGSL AALGAATDSP AHSTELAVLI AANLAATVLR FLLFRAWVFP DRGDQRPYED
PHEDPHEQPY GRSYEQSYEQ PHRTTRFRTG EAADGPWRDT TDATVRLQPA RRRDTDPGDA
R
//
