AGLB_METJA
ID AGLB_METJA Reviewed; 933 AA.
AC Q58920;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase;
DE EC=2.4.99.21;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB; OrderedLocusNames=MJ1525;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in
CC Methanococci) 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. Involved
CC in the assembly of an N-linked disaccharide that decorates the S-layer
CC glycoprotein and flagellins. {ECO:0000250|UniProtKB:Q2EMT4}.
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:Q2EMT4};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000250|UniProtKB:Q2EMT4}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q2EMT4}.
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; L77117; AAB99543.1; -; Genomic_DNA.
DR PIR; D64490; D64490.
DR AlphaFoldDB; Q58920; -.
DR STRING; 243232.MJ_1525; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR EnsemblBacteria; AAB99543; AAB99543; MJ_1525.
DR KEGG; mja:MJ_1525; -.
DR eggNOG; arCOG02044; Archaea.
DR HOGENOM; CLU_018380_0_0_2; -.
DR InParanoid; Q58920; -.
DR OMA; WDNGHIY; -.
DR BRENDA; 2.4.99.18; 3260.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000000805; 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 GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
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..933
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase"
FT /id="PRO_0000107392"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..146
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..263
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..427
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..479
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..933
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 629..631
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 72..74
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 200..202
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 410..413
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 629..633
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT MOTIF 756..763
FT /note="MI motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 413
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 479
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 74
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 193
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 413
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 759
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
SQ SEQUENCE 933 AA; 103964 MW; F3B555913A77379C CRC64;
MYIKVKLMSN ALEKINNFFK EKSWIKVFLI ILMLMFVSFQ LRAQTADMKF AQDNEFLKDM
FSDEHGRMYL LALDPYYYLR LSENLYNNGH CGDTIKVVDG KETPYDLYQY APPGHPLPWE
PPVICLATLA IYYIWHSIDL TVTIMNAAFW VPAVLGMLLG IPIYFVVRRV TNSNIGGIAG
AIALISAPGL LYKTCAGFAD TPIFEVLPIL FIVWFILESI HSQEKTALFK KDLKNPISLF
VIAALIIELI IGAYLNIASG ESVVIASILF YTVSLAFILA GLIIAGIKKL KGNELEFELF
ALLAVILTAV SPKMWGAWWY GFDVITAFLV IYIIALALLK SQVKIKEFIN IGNLKNIVYL
SIFYIFGSFV LLVAIYGMGI AISPITSPLG YNQILSTYTQ TTGWPNVYTT VAELAKPSSW
SEIFTNAIGS DTIAIVGILG ILLSFLSLRY EKVKLDIKYS ILLAIWLAVT LYAATKGIRF
AALATPPLAI GLGIFVGQLE RFLKMKSDIA IFGIGIPAGI FGLLILSKYS AKISQILLPT
TYVPIIAYGF LIVLALLAIY KISDIISTLN DKKETIIKVS TLLLCIGVVI PPLSAVVPFS
VAPTFNNGWK EGLDWIKANT PNNSVITCWW DNGHIYTYEA RRMVTFDGGS QNSPRAYWVG
RAFATSNENL SIGIIRMLAT SGDEAFKKGS VLMNFTHNNV SKTVKILNEI LPVDRSKAYD
ILTKKYGLSD KKAKLVLNAT HPEHPNPDYL ITYNRMTDIA PVWSMFGFWN FSLPPNTPND
KREKGAFFKG TAYYLGNGTI LANVNVYTYS YVTLINSTNI STAIVQKING QAKIIGTFKI
HKLYIKTPLG VKELVLNKDG QLSEFIRIEA DGRGYAWLAT RNLEDSIYAK LHFLDGYGLK
HIKLVKATID PTDFGIQPGF KIYKVDYGTD YLK
