ID   GPT_SULAC               Reviewed;         328 AA.
AC   P39465; Q4JCF9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE            EC=2.7.8.15;
DE   AltName: Full=GlcNAc-1-P transferase;
DE            Short=G1PT;
DE            Short=GPT;
DE   AltName: Full=N-acetylglucosamine-1-phosphate transferase;
GN   Name=gnpTA; OrderedLocusNames=Saci_0093;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=8182085; DOI=10.1016/s0021-9258(17)36694-2;
RA   Ohnuma S., Suzuki M., Nishino T.;
RT   "Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning,
RT   sequencing, and characterization of geranylgeranyl-diphosphate synthase.";
RL   J. Biol. Chem. 269:14792-14797(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-
CC         acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP;
CC         Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:58427; EC=2.7.8.15;
CC   -!- ACTIVITY REGULATION: Inhibited by tunicamycin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
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DR   EMBL; D28748; BAA05941.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY79520.1; -; Genomic_DNA.
DR   PIR; B54058; B54058.
DR   RefSeq; WP_011277021.1; NC_007181.1.
DR   AlphaFoldDB; P39465; -.
DR   SMR; P39465; -.
DR   STRING; 330779.Saci_0093; -.
DR   DNASU; 3473869; -.
DR   EnsemblBacteria; AAY79520; AAY79520; Saci_0093.
DR   GeneID; 3473869; -.
DR   KEGG; sai:Saci_0093; -.
DR   PATRIC; fig|330779.12.peg.88; -.
DR   eggNOG; arCOG03199; Archaea.
DR   HOGENOM; CLU_023982_4_0_2; -.
DR   OMA; DDILGWK; -.
DR   BRENDA; 2.7.8.15; 6160.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR   GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   PANTHER; PTHR22926; PTHR22926; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..328
FT                   /note="Putative UDP-N-acetylglucosamine--dolichyl-phosphate
FT                   N-acetylglucosaminephosphotransferase"
FT                   /id="PRO_0000108766"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   328 AA;  35472 MW;  01798FA2BD3297D9 CRC64;
     MLVSLLGILL SVIVGFVVTL ISTKWVIGLC KKRGFTGKDI NKLTKDDVPV LGGIGIVAGF
     VAGSFTFLLT SYNLSPGIEN VVVSILLSSL IIGFLGLLDD IFNISQATRA FLPIFASIPL
     ILYSVGHTII SIPFLGKVNF GILFYIIILP ATLTITANAF NMLEGLNGLG AGMGLIMALA
     LAYIGLKSGG TSFYAGIVSI ILASVLFGFL IFNFYPAKTF PGNIGTYFIG SVIGSIGISG
     YMYTALFFLY LPYVIEFVLK AKTRFKGVSF GKIDDQGYLH WDSKPNSLTH IVMRIGKFKE
     YHIVLIIWGI EILFAILAVV FQTVTITI