AGLB2_PYRFU
ID AGLB2_PYRFU Reviewed; 743 AA.
AC Q8U3P6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 2;
DE EC=2.4.99.21;
DE AltName: Full=Archaeal glycosylation protein B;
DE Short=AglB-S;
DE Short=AglB-Short;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB2; OrderedLocusNames=PF0411;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE.
RX PubMed=27015803; DOI=10.1074/jbc.m115.713156;
RA Taguchi Y., Fujinami D., Kohda D.;
RT "Comparative analysis of archaeal lipid-linked oligosaccharides that serve
RT as oligosaccharide donors for Asn glycosylation.";
RL J. Biol. Chem. 291:11042-11054(2016).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in
CC P.furiosus) from the lipid carrier dolichol-monophosphate to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent
CC polypeptide chains, the first step in protein N-glycosylation.
CC {ECO:0000250|UniProtKB:Q8U4D2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an archaeal dolichyl phosphooligosaccharide + [protein]-L-
CC asparagine = an archaeal dolichyl phosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.; EC=2.4.99.21;
CC Evidence={ECO:0000250|UniProtKB:Q8U4D2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8U4D2};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8U4D2};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8U4D2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2EMT4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q2EMT4}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:O29867}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL80535.1; -; Genomic_DNA.
DR RefSeq; WP_011011525.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U3P6; -.
DR STRING; 186497.PF0411; -.
DR EnsemblBacteria; AAL80535; AAL80535; PF0411.
DR GeneID; 41712207; -.
DR KEGG; pfu:PF0411; -.
DR PATRIC; fig|186497.12.peg.427; -.
DR eggNOG; arCOG02044; Archaea.
DR HOGENOM; CLU_355503_0_0_2; -.
DR OMA; FWYSVAL; -.
DR OrthoDB; 5183at2157; -.
DR PhylomeDB; Q8U3P6; -.
DR BRENDA; 2.4.99.18; 5243.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001013; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 2.
DR Pfam; PF02516; STT3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..743
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 2"
FT /id="PRO_0000445591"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..91
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..144
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..345
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..394
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..743
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 474..476
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 29..31
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 144..146
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 333..336
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 474..478
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:Q8U4D2"
FT MOTIF 526..533
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:Q8U4D2"
FT BINDING 31
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 394
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 31
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 137
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 336
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 529
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
SQ SEQUENCE 743 AA; 84342 MW; 37A7E2B93A72ABC3 CRC64;
MKIDKRLMVI VAIATLFRMI PFRLKYLVGS DPYFHLAYIE EALKAGEWFN FFTYAGGPWG
LQVRLFHPLG LWATPAYIYK LFSFLGISLY TAFRVTPVIF GVLTVVFFYL SLKKLYNRDV
AFIVGLFLGV NYGHIFRSMA NYYRGDNYML FWYSVALLGI ALGLKTRSKY RYLFYLLPGI
ATGFASAFWQ AYYPIFVFVL AGGLLLGVYA YLKSPKLFLD SILIVLSTGL GVLIANILGD
KVGYGMLGYT DWMGKKVAET FGLEFGFIKD AYLLIHVKYL LPLSLVFLGF LIITKKLNPK
IKVGVLVGGS ILAFIVMLVK FPALKDLSTG FGTFREVPIS ETLPPTLDDL WRAYNIAIFL
AALYILRLRK IRSGDAILLG YVITSLWMLR YWTRFLFTAA PAVAFLSGIG VYELTRRIKE
NKIRITSLGV VILLSSAFSL GEVYSVKPFM NENWEKALIF IRENSNENDI VLTWWDWGHF
VTYYARRSPV AQGSPNSGVA GYYLGLVDNG WAQSLGVDYV IVSLYDILKF EAIVDTAKLS
RKWENISRAD YGVDFLKLTE STGSILRFDS QYSTLIVKEG NIRVILSGKV VYPREAIIES
NGRIKNLKYP ARSGVYVYVN LDYGYAILAN EKAWETNLLR LFTQRTGENY ELVYSDGGFV
KVFRFVHPNV VFRGNKFILT GNGTGLGLYG YLDNGTLVFK KWYSVKNMQE FELPNNLNGS
VVVRYVYTQG KIVLDRGIVR VKN
