ID A0A2R4T5L6_9ACTN Unreviewed; 828 AA.
AC A0A2R4T5L6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN ORFNames=SLUN_21615 {ECO:0000313|EMBL:AVZ74374.1};
OS Streptomyces lunaelactis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1535768 {ECO:0000313|EMBL:AVZ74374.1, ECO:0000313|Proteomes:UP000244201};
RN [1] {ECO:0000313|EMBL:AVZ74374.1, ECO:0000313|Proteomes:UP000244201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM109 {ECO:0000313|EMBL:AVZ74374.1,
RC ECO:0000313|Proteomes:UP000244201};
RA Naome A., Martinet L., Maciejewska M., Anderssen S., Adam D., Tenconi E.,
RA Deflandre B., Arguelles-Arias A., Calusinska M., Copieters W., Karim L.,
RA Hanikenne M., Baurain D., van Wezel G., Smargiasso N., de Pauw E.,
RA Delfosse P., Rigali S.;
RT "Complete genome sequence of Streptomyces lunaelactis MM109T, a Ferroverdin
RT A producer isolated from cave moonmilk deposits.";
RL Submitted (JAN-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}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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DR EMBL; CP026304; AVZ74374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4T5L6; -.
DR KEGG; slk:SLUN_21615; -.
DR OrthoDB; 2369748at2; -.
DR Proteomes; UP000244201; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd04188; DPG_synthase; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
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 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000244201};
KW Transferase {ECO:0000313|EMBL:AVZ74374.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..186
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 828 AA; 89721 MW; 6578CF8D46BEB1B4 CRC64;
MSAQAQAPVY AGAYPHADVD LTVVVPAYNE EARLRPTLDA ICAHLRAEPG RWGSWELIVV
DDGSTDATAK IAREAAAEEP RIHVVAGDGN RGKGSALRLG VLASYGRRVL ITDADLATPI
EELDRLDKQL AAEDSAAAIG SRAHPDSRIE VHQRRTREWL GRMGNHLIRA VAVPGILDTQ
CGFKLFDGDK ARAAFADSRL DGWGIDVEIL RFFRREGWPV TEVPVRWSHR AGSKVRPLDY
GRVLLELVRL RARAVRRVDL AVTGLVLLAS VLLYKGLWAD LDGSYLVDAG QDQNQWQWFF
AVTADNVAHL RNPLFTTLQG YPDGVNLMAN TVMLGLSVPL TPVTLLFGPS VTWALVLTLG
LAATATAWYW LIARRLVRNR WAAALGGAFA AFAPPMISHG NAHPNFLVLF MIPVIIDRAL
RLCEAGRGGR TVVRDGVLLG LFATYQIFLG EEPLLLAAMG MLLFALSYAL ARPDVARAAW
RPLLRGLGVA AVVCLPLVAF PLGWQFFGPQ SYKSVLHGDN MGNSPLAFLE FAGRSLAGSD
EGADPLAFNR TEQNAFYGWP LIALAAAIVV RLWRSALVKA LAFTALAAAL LSLGPKFRIP
YTDTVLTGPW RALAHQPLFE SVIESRVAMI CAPVLGVLLA LAADRLLLTR RRVNQVVGLA
AVAAAVLPVL PTPYPVRERS EVPAFVTEGM YRGYLAEGES VVTVPLPYPG SAEALHWQSS
TGLGFPVAGG YFNGPWGPER MGIYGATPRH TSNLLNDVRN SGRVPVIGPN WQAQARSDLA
AWKAGVVVLA PQYNDRALYT TVEKLLGRPG KPVGGVWVWD VGEPRSSG
//
