AGLB_HALVD
ID AGLB_HALVD Reviewed; 1054 AA.
AC D4GYH4; A9JPF0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Dolichyl-monophosphooligosaccharide--protein glycotransferase AglB;
DE EC=2.4.99.21 {ECO:0000269|PubMed:21091511};
DE AltName: Full=Archaeal glycosylation protein B;
DE AltName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
DE AltName: Full=Oligosaccharyl transferase AglB;
GN Name=aglB; OrderedLocusNames=HVO_1530;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN GLYCOSYLATION, PATHWAY, AND
RP GENE NAME.
RC STRAIN=DS2 / DS70;
RX PubMed=17996897; DOI=10.1016/j.jmb.2007.10.042;
RA Abu-Qarn M., Yurist-Doutsch S., Giordana A., Trauner A., Morris H.R.,
RA Hitchen P., Medalia O., Dell A., Eichler J.;
RT "Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-
RT layer glycoprotein and proper assembly of the surface layer.";
RL J. Mol. Biol. 374:1224-1236(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21091511; DOI=10.1111/j.1365-2958.2010.07405.x;
RA Guan Z., Naparstek S., Kaminski L., Konrad Z., Eichler J.;
RT "Distinct glycan-charged phosphodolichol carriers are required for the
RT assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer
RT glycoprotein.";
RL Mol. Microbiol. 78:1294-1303(2010).
RN [4]
RP PROBABLE FUNCTION IN GLYCOSYLATION OF FLAGELLINS.
RC STRAIN=H53;
RX PubMed=22730124; DOI=10.1128/jb.00731-12;
RA Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.;
RT "N-glycosylation of Haloferax volcanii flagellins requires known Agl
RT proteins and is essential for biosynthesis of stable flagella.";
RL J. Bacteriol. 194:4876-4887(2012).
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 (a hexose-linked tetrasaccharide composed
CC of a hexose, 2 hexuronic acids and a methyl ester of hexuronic acid in
CC H.volcanii) 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 (Probable). Involved in the assembly of an N-linked pentasaccharide
CC that decorates the S-layer glycoprotein and flagellins
CC (PubMed:17996897, PubMed:21091511) (Probable).
CC {ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:21091511,
CC ECO:0000305|PubMed:22730124, 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:21091511};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:17996897}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:17996897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AM922226; CAP58184.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03209.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GYH4; -.
DR SMR; D4GYH4; -.
DR STRING; 309800.C498_03005; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR TCDB; 9.B.142.3.15; the integral membrane glycosyltransferase family 39 (gt39) family.
DR EnsemblBacteria; ADE03209; ADE03209; HVO_1530.
DR KEGG; hvo:HVO_1530; -.
DR eggNOG; arCOG02043; Archaea.
DR HOGENOM; CLU_008803_0_0_2; -.
DR OMA; SWYHWRT; -.
DR BioCyc; MetaCyc:MON-19288; -.
DR BRENDA; 2.4.99.21; 2561.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; 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: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; IDA:UniProtKB.
DR InterPro; IPR041154; AglB_P1.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR026410; OlisacTrfase_arch.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF18079; AglB_L1; 1.
DR Pfam; PF02516; STT3; 1.
DR TIGRFAMs; TIGR04154; archaeo_STT3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1054
FT /note="Dolichyl-monophosphooligosaccharide--protein
FT glycotransferase AglB"
FT /id="PRO_0000415386"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..118
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..174
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..237
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..295
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..396
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..1054
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 638..640
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT REGION 1005..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..55
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 172..174
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 373..376
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 638..642
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 701..712
FT /note="DKi motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT COMPBIAS 1015..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 173
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 504
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 55
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 165
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 376
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 708
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
SQ SEQUENCE 1054 AA; 113675 MW; 855F63B0810835E8 CRC64;
MSDEQTKYSP SIAELARDWY HIPVLSTIIL VMLWIRLRSY DAFIREGTVF FSGNDAWYHL
RQVEYTVRNW PATMPFDPWT EFPFGRTAGQ FGTIYDQLVA TAALVVGLGS PSSDLVAKSL
LVAPAVFGAL TVIPTYLIGK RLGGRLGGLF GAVILMLLPG TFLQRGLVGF ADHNIVEPFF
MGFAVLAIMI ALTVADREKP VWELVAARDL DALREPLKWS VLAGVATAIY MWSWPPGILL
VGIFGLFLVL KMASDYVRGR SPEHTAFVGA ISMTVTGLLM FIPIEEPGFG VTDFGFLQPL
FSLGVALGAV FLAALARWWE SNDVDERYYP AVVGGTMLVG IVLFSLVLPS VFDSIARNFL
RTVGFSAGAA TRTISEAQPF LAANVLQSNG QTAVGRIMSE YGFTFFTGAL AAVWLVAKPL
VKGGNSRKIG YAVGSLALIG VLFLIPALPA GIGSALGVEP SLVSLTIVTA LIVGAVMQAD
YESERLFVLV WAAIITSAAF TQVRFNYYLA VVVAVMNAYL LREALGIDFV GLANVERFDD
ISYGQVAAVV IAVLLILTPV LIIPIQLGNG GVSQTAMQAS QTGPGTVTQW DGSLTWMQNN
TPAEGEFGGE SNRMEYYGTY EYTDDFDYPD GAYGVMSWWD YGHWITVLGE RIPNANPFQG
GATEAANYLL AEDEQQAESV LTSMGDDGEG DQTRYVMVDW QMASTDAKFS APTVFYDESN
ISRSDFYNPM FRLQEQGEQT TVAAASSLKD QRYYESLMVR LYAYHGSARE ASPIVVDWEE
RTSADGSTTF RVTPSDGQAV RTFDNMSAAE EYVANDPTSQ IGGIGTFPEE RVSALEHYRL
VKSSNSSALR SGSYQRSLIS EGNTYGLQPQ ALVPNNPAWV KTFERVPGAT VDGSGAPANT
TVTARVQMRD LTTGTNFTYT QQAQTDADGE FTMTLPYSTT GYDEYGPDNG YTNVSVRAAG
GYAFTGPTSV TGNSTIVSYQ AENVAVDEGL VNGAEDGTVQ VTLERNEQEL DLPGDSSSED
SSSEDGTSDG SQTNESASTS TSASVDASAV SAAA
