GPT_SACS2
ID GPT_SACS2 Reviewed; 322 AA.
AC P96000;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=SSO0060; ORFNames=C05011;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; Y08257; CAA69542.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40422.1; -; Genomic_DNA.
DR PIR; S75428; S75428.
DR RefSeq; WP_009988861.1; NC_002754.1.
DR AlphaFoldDB; P96000; -.
DR SMR; P96000; -.
DR STRING; 273057.SSO0060; -.
DR DNASU; 1455313; -.
DR EnsemblBacteria; AAK40422; AAK40422; SSO0060.
DR GeneID; 44129023; -.
DR KEGG; sso:SSO0060; -.
DR PATRIC; fig|273057.12.peg.61; -.
DR eggNOG; arCOG03199; Archaea.
DR HOGENOM; CLU_023982_4_0_2; -.
DR InParanoid; P96000; -.
DR OMA; DDILGWK; -.
DR PhylomeDB; P96000; -.
DR PRO; PR:P96000; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IBA:GO_Central.
DR GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
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..322
FT /note="Putative UDP-N-acetylglucosamine--dolichyl-phosphate
FT N-acetylglucosaminephosphotransferase"
FT /id="PRO_0000108767"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 322 AA; 35252 MW; 41F58B03A3269F7D CRC64;
MRILAILLPI LISFFISYIT TVWVIRQAKK SRFVGKDINK PDKPEIPLLG GIGIIAGFIA
GSFSLLLTDV RSERVIPAVI LSSLLIAFLG LLDDIFNVRQ SVRAFLPIFA SVPLIVYSVG
HSIISIPFLG PINFGIFYYI IIIPFALTIT SNAFNMLEGL NGLGVGMGII MLSALAYIGL
THTGPTYQAG LIALSAIFSL SAFLIFNKYP AKIFPGNVGT YFIGALIGAI GIAGFMYTAL
AILYIPYVVE FILKLRTNFK GVSFGKVDSS GRLYWDEKPH SLTHIVMKMG RFKEYQVVII
LWGMEAIFAV IAVILQTTTI VI
