ID   A9AVM1_HERA2            Unreviewed;       238 AA.
AC   A9AVM1;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   02-SEP-2026, entry version 80.
DE   RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE            EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN   OrderedLocusNames=Haur_3989 {ECO:0000313|EMBL:ABX06621.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX06621.1, ECO:0000313|Proteomes:UP000000787};
RN   [1] {ECO:0000313|EMBL:ABX06621.1, ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RX   PubMed=22675585; DOI=10.4056/sigs.2194987;
RA   Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA   Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA   Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT   "Complete genome sequence of the filamentous gliding predatory bacterium
RT   Herpetosiphon aurantiacus type strain (114-95(T)).";
RL   Stand. Genomic Sci. 5:356-370(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl phosphate + UDP-alpha-D-glucose =
CC         a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + UDP;
CC         Xref=Rhea:RHEA:15401, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502,
CC         ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.117;
CC         Evidence={ECO:0000256|ARBA:ARBA00045097};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15402;
CC         Evidence={ECO:0000256|ARBA:ARBA00045097};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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DR   EMBL; CP000875; ABX06621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AVM1; -.
DR   FunCoup; A9AVM1; 446.
DR   STRING; 316274.Haur_3989; -.
DR   KEGG; hau:Haur_3989; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_033536_9_0_0; -.
DR   InParanoid; A9AVM1; -.
DR   BioCyc; HAUR316274:GHYA-4031-MONOMER; -.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR   CDD; cd04188; DPG_synthase; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000787};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABX06621.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          10..177
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   238 AA;  27560 MW;  ED992E1ECB374CB7 CRC64;
     MAHTDYSVDI VIPVLNEEQQ LEQSVVALRD FLQASCPYRW RIVVADNGST DRTPQICHDL
     RSRFPGEVDF ERLEQRGRGR ALRTAWLKSS ADILCYMDVD LSTNLRALPP LLAALIHSDY
     SLGTGSRLMH GAIVTRQWKR EMISRAYNLL IRVLFWHRFR DAQCGFKAIT RQAAQELIPM
     VRDNEWFFDT ELLLKAERRG YRIFEVPVEW IEDLGTTVKI VKTAWQDIKG LVRVRLGG
//