AGLB_METVO
ID AGLB_METVO Reviewed; 917 AA.
AC Q2EMT4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase {ECO:0000303|PubMed:23624439};
DE EC=2.4.99.21 {ECO:0000269|PubMed:23624439};
DE AltName: Full=Oligosaccharyl transferase {ECO:0000303|PubMed:23624439};
DE Short=OST {ECO:0000303|PubMed:24212570};
DE Short=OTase {ECO:0000303|PubMed:23624439};
GN Name=aglB {ECO:0000303|PubMed:16824110}; ORFNames=MVO1749;
OS Methanococcus voltae.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2188;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RA Bhattacharyya A., Overbeek R., Jarrell K., Chaban B., Whitman W.;
RT "Partial sequence of Methanococcus voltae genome.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX PubMed=16824110; DOI=10.1111/j.1365-2958.2006.05226.x;
RA Chaban B., Voisin S., Kelly J., Logan S.M., Jarrell K.F.;
RT "Identification of genes involved in the biosynthesis and attachment of
RT Methanococcus voltae N-linked glycans: insight into N-linked glycosylation
RT pathways in Archaea.";
RL Mol. Microbiol. 61:259-268(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX PubMed=23624439; DOI=10.1038/nchembio.1249;
RA Larkin A., Chang M.M., Whitworth G.E., Imperiali B.;
RT "Biochemical evidence for an alternate pathway in N-linked glycoprotein
RT biosynthesis.";
RL Nat. Chem. Biol. 9:367-373(2013).
RN [4]
RP FUNCTION.
RX PubMed=24212570; DOI=10.1128/aem.03191-13;
RA Cohen-Rosenzweig C., Guan Z., Shaanan B., Eichler J.;
RT "Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can
RT process a variety of lipid-linked glycans.";
RL Appl. Environ. Microbiol. 80:486-496(2014).
RN [5]
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 (ManNAcGlc-2,3-diNAcAGlcNAc in M.voltae)
CC from the lipid carrier dolichol-monophosphate to an asparagine residue
CC within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains,
CC the first step in protein N-glycosylation (PubMed:24212570) (Probable).
CC Involved in the assembly of an N-linked disaccharide that decorates the
CC S-layer glycoprotein and flagellins (PubMed:16824110, PubMed:23624439).
CC {ECO:0000269|PubMed:16824110, ECO:0000269|PubMed:23624439,
CC ECO:0000269|PubMed:24212570, ECO:0000305|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:0000269|PubMed:23624439};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23624439};
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:0000305|PubMed:16824110}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:16824110}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23624439};
CC Multi-pass membrane protein {ECO:0000305|PubMed:23624439}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene result in flagellins and
CC S-layer proteins with significantly reduced apparent molecular masses,
CC loss of flagellar assembly and absence of glycan attachment.
CC {ECO:0000269|PubMed:16824110}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; DQ372942; ABD17750.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2EMT4; -.
DR KEGG; ag:ABD17750; -.
DR BioCyc; MetaCyc:MON-19266; -.
DR BRENDA; 2.4.99.21; 3268.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
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:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
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; IMP:UniProtKB.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 2.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Metal-binding; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..917
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase"
FT /id="PRO_0000435653"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..209
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..263
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..372
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..438
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..506
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..917
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..594
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 82..84
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 208..210
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 361..364
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 592..596
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT MOTIF 719..726
FT /note="MI motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 438
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 84
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 201
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 364
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 722
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
SQ SEQUENCE 917 AA; 102424 MW; C27FDF67C1376C8C CRC64;
MTENNEKVKN SDSANNQSSK NSKFNFNFED KKVKCAKTIL IIIFLAFLSF QMRAQTADMG
FTTNEQYLDV FSDDNGRMYL TALDPYYYLR MSENYLENGH TGDTLKNIDG QQVPWDSYKY
GPTGARATFN LLSVVTVWVY QVWHAMDSTV TLMNAAFWVP AILSMFLITP IFFTVRRITS
SDIGGAVAAI LASLSPSIFV KTVAGFSDTP ILEILPLLFI VWFIIEAIHY SKEKNYKSLI
YGLLATLMLA LYPFMWSAWW YGYYIVIAFL VIYAIYKGIS YNSIAKYTKS KNNNHKDKIE
SEKLEMLNIL KISGLFIIGG AVLITALYGV STTMNALQAP LNYLGLDEVS SQTGWPNVLT
TVSELDTASL DEIISSSLGS IHLFAIGLIG IFLSLFRKVL TPVKQISNGL AEKLDIKYAL
LLIIWFAVTF LAASKGVRFV ALMVPPLSIG VGIFVGFIEQ FIKNNLDKKY EYVAYPTIAI
IVLYALFTIY RADSADLVRM LLPSNYVPIA EGIMLASLAV LIIYKVAELI AESNKKLVMN
KIFMILLAIG LITPTIATIV PFYSVPTYND GWGESLEWIN TQTPNNSVVT CWWDNGHIYT
WKTDRMVTFD GSSQNTPRAY WVGRAFSTSN ESLANGIFRM LASSGDKAYT TDSVLIKKTG
SIKNTVDVLN EILPLTKSDA QKALKNSSYK FTDTEVSEIL DATHPKVTNP DYLITYNRMT
SIASVWSYFG NWDFNLPAGT SRSEREAGSF QGLQTYATNI NDTLIVRSLI QQTAEYNIYT
LIEVRNETLT GAMMAVTNDG QMQTQQLNMH KVKLMVNENG KSKMYNSLAD PDGQLSLLIK
VDKNSIIGTD GSNNPVYSSS SWMATANLED SVYSKLHFFD GEGLDTIKLE KESLDPTANG
VQPGFKVFSV DYGNYSK
