AGLB2_ARCFU
ID AGLB2_ARCFU Reviewed; 593 AA.
AC O30195;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 2;
DE EC=2.4.99.21;
DE AltName: Full=Archaeal glycosylation protein B;
DE Short=AglB-S2;
DE Short=AglB-Short 2;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB2; OrderedLocusNames=AF_0040;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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).
RN [3] {ECO:0007744|PDB:3VU0}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 433-593.
RX PubMed=23177926; DOI=10.1016/j.str.2012.10.011;
RA Nyirenda J., Matsumoto S., Saitoh T., Maita N., Noda N.N., Inagaki F.,
RA Kohda D.;
RT "Crystallographic and NMR evidence for flexibility in
RT oligosaccharyltransferases and its catalytic significance.";
RL Structure 21:32-41(2013).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (a GalNAc-linked heptasaccharide composed
CC of 4 Hex, 3 dHex and a sulfate for A.fulgidus AglB-S) from the lipid
CC carrier dolichol-monophosphate to an asparagine residue within an Asn-
CC X-Ser/Thr consensus motif in nascent polypeptide chains, the first step
CC in protein N-glycosylation. {ECO:0000269|PubMed:27015803}.
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:Q2EMT4};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:27015803}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2EMT4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q2EMT4}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB91198.1; -; Genomic_DNA.
DR PIR; H69254; H69254.
DR PDB; 3VU0; X-ray; 1.94 A; A/B/C=433-593.
DR PDBsum; 3VU0; -.
DR AlphaFoldDB; O30195; -.
DR SMR; O30195; -.
DR STRING; 224325.AF_0040; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR EnsemblBacteria; AAB91198; AAB91198; AF_0040.
DR KEGG; afu:AF_0040; -.
DR eggNOG; arCOG02043; Archaea.
DR HOGENOM; CLU_008803_0_0_2; -.
DR OMA; VAYSSWY; -.
DR PhylomeDB; O30195; -.
DR BRENDA; 2.4.99.18; 414.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002199; 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; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycosyltransferase; Magnesium; Manganese;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..593
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 2"
FT /id="PRO_0000445595"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..98
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..229
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..310
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..593
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 468..470
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 41..43
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 153..155
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 302..305
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 468..472
FT /note="WWDYG motif"
FT /evidence="ECO:0000305|PubMed:23177926"
FT MOTIF 524..539
FT /note="DKi motif"
FT /evidence="ECO:0000305|PubMed:23177926"
FT BINDING 43
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 154
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 354
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 43
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 146
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 305
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 535
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:3VU0"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:3VU0"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:3VU0"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 492..500
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:3VU0"
FT STRAND 516..522
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 536..543
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 552..559
FT /evidence="ECO:0007829|PDB:3VU0"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:3VU0"
FT TURN 569..574
FT /evidence="ECO:0007829|PDB:3VU0"
FT STRAND 576..584
FT /evidence="ECO:0007829|PDB:3VU0"
FT STRAND 587..592
FT /evidence="ECO:0007829|PDB:3VU0"
SQ SEQUENCE 593 AA; 68172 MW; 84F12A506A649088 CRC64;
MTPVGMDRKS LSLLILIVLL GLCIRLQNFG EIFDSRIYYY GYDPYYHMRL VEAIVLEGYR
PSFDYYINYP YGLRIDWLPL FDYILAFPGL FLGFWASEIF AVVFPVIIGV LCIVLVYLIS
LEVLRNEKFA LISAFIFSVC PVTVWKSLLG KADHHIWVVF LLLLSIWLVT KPGLLKLLSG
IPMLLMALSW LGAPIYAALL AVSSLFQFNE KEVRIVGISN LIPVLSSIQN LFLGFSFLAI
AVFLLVGSFV KRFERRFRYA IVYYLCICSV ALLSAYLMPV GWLGFVKSGI SYVLGTDIYL
PTIREARSFQ ILGVISSAGY LFFVLAIPAL FMLRNGFLKV FFVLSFLISI LQLRFVEVLA
FPVAILASYT ICQILERVDY PVFRKEEEGE SKRRGRKEKK KAVEIRKKDH ATVIAFLLFL
ALPCFANSLA PVEMTMDWKE ALNWMKENLE AQDYLKAYEK PDYAVLSWWD YGNWILYVAK
KAVVCNNFQA GADDAAKFFT AQSEEEAMKI VEKRKVRYVV TVEELTVKPE TNKTKFIPIM
QIAGYSPEYM KNKEIIDFFN KTMLYKLHVE NATNLTHFRL LKNFGTVKIF EVK
