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Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.19) (Protein glycosylation B)

 PGLB_CAMJR              Reviewed;         713 AA.
Q5HTX9;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
05-DEC-2018, entry version 67.
RecName: Full=Undecaprenyl-diphosphooligosaccharide--protein glycotransferase;
EC=2.4.99.19 {ECO:0000269|PubMed:20007322};
AltName: Full=Protein glycosylation B;
Name=pglB; OrderedLocusNames=CJE1268;
Campylobacter jejuni (strain RM1221).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=195099;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RM1221;
PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms
from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
[2]
DOMAIN.
PubMed=21812456; DOI=10.1021/bi201018d;
Jaffee M.B., Imperiali B.;
"Exploiting topological constraints to reveal buried sequence motifs
in the membrane-bound N-linked oligosaccharyl transferases.";
Biochemistry 50:7557-7567(2011).
[3]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 428-713, FUNCTION, AND
MUTAGENESIS OF SER-52; ASN-53; ASP-54; MET-568; SER-569; LEU-570 AND
ILE-571.
STRAIN=RM1221;
PubMed=20007322; DOI=10.1074/jbc.M109.081752;
Maita N., Nyirenda J., Igura M., Kamishikiryo J., Kohda D.;
"Comparative structural biology of eubacterial and archaeal
oligosaccharyltransferases.";
J. Biol. Chem. 285:4941-4950(2010).
-!- FUNCTION: Oligosaccharyltransferase that catalyzes the transfer of
a preassembled heptasaccharide from a lipid donor to an asparagine
residue in nascent polypeptide chains, affording a beta-linked
glycan to the asparagine side chain of target proteins.
{ECO:0000269|PubMed:20007322}.
-!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the
initial transfer of a defined glycan
(GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2)
is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-
pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-
Ser/Thr consensus motif in nascent polypeptide chains, the first
step in protein N-glycosylation. {ECO:0000250|UniProtKB:B9KDD4}.
-!- CATALYTIC ACTIVITY:
Reaction=Tritrans,heptacis-undecaprenyl diphosphooligosaccharide +
[protein]-L-asparagine = tritrans,heptacis-undecaprenyl
diphosphate + a glycoprotein with the oligosaccharide chain
attached by N-beta-D-glycosyl linkage to protein L-asparagine.;
EC=2.4.99.19; Evidence={ECO:0000269|PubMed:20007322};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:B9KDD4};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:B9KDD4};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:B9KDD4}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000250|UniProtKB:B9KDD4}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:B9KDD4}.
-!- DOMAIN: Despite low primary sequence conservation between
eukaryotic catalytic subunits and bacterial and archaeal single
subunit OSTs (ssOST), structural comparison revealed several
common motifs at spatially equivalent positions, like the DXD
motif 1 on the external loop 1 and the DXD motif 2 on the external
loop 2 involved in binding of the metal ion cofactor and the
carboxamide group of the acceptor asparagine, the conserved Glu
residue of the TIXE/SVSE motif on the external loop 5 involved in
catalysis, as well as the WWDYG and the DK/MI motifs in the
globular domain that define the binding pocket for the +2 Ser/Thr
of the acceptor sequon. In bacterial ssOSTs, an Arg residue was
found to interact with a negatively charged side chain at the -2
position of the sequon. This Arg is conserved in bacterial enzymes
and correlates with an extended sequon requirement (Asp-X-Asn-X-
Ser/Thr) for bacterial N-glycosylation.
{ECO:0000250|UniProtKB:B9KDD4}.
-!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CP000025; AAW35590.1; -; Genomic_DNA.
RefSeq; WP_011049884.1; NC_003912.7.
PDB; 3AAG; X-ray; 2.80 A; A/B=428-713.
PDBsum; 3AAG; -.
SMR; Q5HTX9; -.
CAZy; GT66; Glycosyltransferase Family 66.
EnsemblBacteria; AAW35590; AAW35590; CJE1268.
KEGG; cjr:CJE1268; -.
HOGENOM; HOG000103852; -.
KO; K17251; -.
OMA; GYPIRYY; -.
BioCyc; CJEJ195099:G1G43-1269-MONOMER; -.
BRENDA; 2.4.99.18; 1087.
BRENDA; 2.4.99.19; 1087.
UniPathway; UPA00378; -.
EvolutionaryTrace; Q5HTX9; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IMP:TIGR.
GO; GO:0006487; P:protein N-linked glycosylation; IMP:TIGR.
InterPro; IPR003674; Oligo_trans_STT3.
Pfam; PF02516; STT3; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Glycoprotein;
Glycosyltransferase; Magnesium; Membrane; Metal-binding; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 713 Undecaprenyl-diphosphooligosaccharide--
protein glycotransferase.
/FTId=PRO_0000422588.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000305}.
TRANSMEM 12 35 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 36 96 Periplasmic. {ECO:0000305}.
TRANSMEM 97 122 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 123 125 Cytoplasmic. {ECO:0000305}.
TRANSMEM 126 144 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 145 152 Periplasmic. {ECO:0000305}.
TRANSMEM 153 174 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 175 176 Cytoplasmic. {ECO:0000305}.
TRANSMEM 177 192 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 193 197 Periplasmic. {ECO:0000305}.
TRANSMEM 198 215 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 216 220 Cytoplasmic. {ECO:0000305}.
TRANSMEM 221 233 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 234 237 Periplasmic. {ECO:0000305}.
TRANSMEM 238 254 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 255 260 Cytoplasmic. {ECO:0000305}.
TRANSMEM 261 278 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 279 324 Periplasmic. {ECO:0000305}.
TRANSMEM 325 347 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 348 352 Cytoplasmic. {ECO:0000305}.
TRANSMEM 353 369 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 370 373 Periplasmic. {ECO:0000305}.
TRANSMEM 374 396 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 397 406 Cytoplasmic. {ECO:0000305}.
TRANSMEM 407 427 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 428 713 Periplasmic. {ECO:0000305}.
REGION 194 196 Lipid-linked oligosaccharide binding.
{ECO:0000250|UniProtKB:B9KDD4}.
REGION 457 459 Target acceptor peptide binding.
{ECO:0000250|UniProtKB:B9KDD4}.
MOTIF 52 54 DXD motif 1.
{ECO:0000305|PubMed:21812456}.
MOTIF 152 154 DXD motif 2.
{ECO:0000305|PubMed:21812456}.
MOTIF 313 316 TIXE motif.
{ECO:0000305|PubMed:21812456}.
MOTIF 457 461 WWDYG motif.
{ECO:0000305|PubMed:21812456}.
MOTIF 568 575 MI motif. {ECO:0000250|UniProtKB:O29918}.
METAL 54 54 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
METAL 152 152 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
METAL 316 316 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 54 54 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 291 291 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 316 316 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 328 328 Target acceptor peptide; important for
extended sequon recognition.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 372 372 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 462 462 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 571 571 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
SITE 145 145 Important for catalytic activity.
{ECO:0000250|UniProtKB:B9KDD4}.
CARBOHYD 534 534 N-linked (DATDGlc) asparagine.
{ECO:0000250|UniProtKB:B9KDD4}.
MUTAGEN 52 52 S->E,D: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:20007322}.
MUTAGEN 53 53 N->A: Reduced catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 54 54 D->A: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:20007322}.
MUTAGEN 568 568 M->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 569 569 S->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 570 570 L->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 571 571 I->A: Strong reduction in catalytic
activity. {ECO:0000269|PubMed:20007322}.
HELIX 437 444 {ECO:0000244|PDB:3AAG}.
STRAND 453 455 {ECO:0000244|PDB:3AAG}.
HELIX 458 460 {ECO:0000244|PDB:3AAG}.
HELIX 461 468 {ECO:0000244|PDB:3AAG}.
HELIX 481 492 {ECO:0000244|PDB:3AAG}.
HELIX 495 510 {ECO:0000244|PDB:3AAG}.
HELIX 525 531 {ECO:0000244|PDB:3AAG}.
TURN 532 534 {ECO:0000244|PDB:3AAG}.
HELIX 538 544 {ECO:0000244|PDB:3AAG}.
STRAND 560 565 {ECO:0000244|PDB:3AAG}.
HELIX 566 570 {ECO:0000244|PDB:3AAG}.
HELIX 572 577 {ECO:0000244|PDB:3AAG}.
STRAND 594 597 {ECO:0000244|PDB:3AAG}.
STRAND 599 601 {ECO:0000244|PDB:3AAG}.
STRAND 606 609 {ECO:0000244|PDB:3AAG}.
STRAND 614 616 {ECO:0000244|PDB:3AAG}.
TURN 624 626 {ECO:0000244|PDB:3AAG}.
STRAND 632 639 {ECO:0000244|PDB:3AAG}.
STRAND 644 649 {ECO:0000244|PDB:3AAG}.
STRAND 657 660 {ECO:0000244|PDB:3AAG}.
STRAND 670 674 {ECO:0000244|PDB:3AAG}.
TURN 678 680 {ECO:0000244|PDB:3AAG}.
HELIX 682 686 {ECO:0000244|PDB:3AAG}.
STRAND 697 699 {ECO:0000244|PDB:3AAG}.
STRAND 704 712 {ECO:0000244|PDB:3AAG}.
SEQUENCE 713 AA; 82206 MW; B5D4836BF36D8FF8 CRC64;
MLKKEYLKNP YLVLFAMIIL AYVFSVLCRF YWIWWASEFN EYFFNNQLMI ISNDGYAFAE
GARDMIAGFH QPNDLSYYGS SLSTLTYWLY KITPFSFESI ILYMSTFLSS LVVIPIILLA
NEYKRPLMGF VAALLASVAN SYYNRTMSGY YDTDMLVIVL PMFILFFMVR MILKKDFFSL
IALPLFIGIY LWWYPSSYTL NVALIGLFLI YTLIFHRKEK IFYIAVILSS LTLSNIAWFY
QSAIIVILFA LFALEQKRLN FMIIGILGSA TLIFLILSGG VDPILYQLKF YIFRNDESAN
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH KSMIMALPIL
VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY SQLTSNVCIV FATILTLAPV
FIHIYNYKAP TVFSQNEASL LNQLKNIANR EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL
GKDNFFPSFA LSKDEQAAAN MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL
FLASLSKPDF KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI DDKAQFYIFY
LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV INSRDAKVFK LKI


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DDR2 DDOST Gene dolichyl-diphosphooligosaccharide--protein glycosyltransferase

Kits Elisa; taq POLYMERASE

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Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[STT3B SIMP] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18) (Source of immunodominant MHC-associated peptides homolog)
[Stt3b Simp] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18) (B6dom1 antigen) (Source of immunodominant MHC-associated peptides)
[STT3B] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B (Oligosaccharyl transferase subunit STT3B) (STT3-B) (EC 2.4.99.18)
[STT3A ITM1 TMC] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (B5) (Integral membrane protein 1) (Transmembrane protein TMC)
[STT3 YGL022W] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 (Oligosaccharyl transferase subunit STT3) (EC 2.4.99.18) (Staurosporine and temperature sensitivity protein 3)
[Stt3a Itm1] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (B5) (Integral membrane protein 1)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[GP1 MZ11_60484gpGP1 MZ11_60553gpGP1] Genome polyprotein [Cleaved into: Peptide 2k; Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[STT3A] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[OST4 YDL232W] Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4 (Oligosaccharyl transferase subunit OST4) (Oligosaccharyl transferase 4 kDa subunit) (OTase 4 kDa subunit)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

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