ID   Q2FTM5_METHJ            Unreviewed;       854 AA.
AC   Q2FTM5;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=dolichyl-phosphooligosaccharide-protein glycotransferase {ECO:0000256|ARBA:ARBA00012602};
DE            EC=2.4.99.21 {ECO:0000256|ARBA:ARBA00012602};
DE   AltName: Full=Oligosaccharyl transferase {ECO:0000256|ARBA:ARBA00030679};
GN   OrderedLocusNames=Mhun_2859 {ECO:0000313|EMBL:ABD42551.1};
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD42551.1, ECO:0000313|Proteomes:UP000001941};
RN   [1] {ECO:0000313|Proteomes:UP000001941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC   {ECO:0000313|Proteomes:UP000001941};
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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:0000256|ARBA:ARBA00034066};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the STT3 family.
CC       {ECO:0000256|ARBA:ARBA00010810}.
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; CP000254; ABD42551.1; -; Genomic_DNA.
DR   RefSeq; WP_011449804.1; NC_007796.1.
DR   AlphaFoldDB; Q2FTM5; -.
DR   FunCoup; Q2FTM5; 96.
DR   STRING; 323259.Mhun_2859; -.
DR   EnsemblBacteria; ABD42551; ABD42551; Mhun_2859.
DR   GeneID; 3923687; -.
DR   KEGG; mhu:Mhun_2859; -.
DR   eggNOG; arCOG02043; Archaea.
DR   HOGENOM; CLU_008803_0_0_2; -.
DR   InParanoid; Q2FTM5; -.
DR   OrthoDB; 82393at2157; -.
DR   BRENDA; 2.4.99.18; 3282.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.60.40.3390; -; 1.
DR   Gene3D; 3.40.50.12610; -; 1.
DR   InterPro; IPR054479; AglB-like_core.
DR   InterPro; IPR041154; AglB_P1.
DR   InterPro; IPR003674; Oligo_trans_STT3.
DR   InterPro; IPR026410; OlisacTrfase_arch.
DR   InterPro; IPR048307; STT3_N.
DR   NCBIfam; TIGR04154; archaeo_STT3; 1.
DR   PANTHER; PTHR13872; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT; 1.
DR   PANTHER; PTHR13872:SF1; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT STT3B; 1.
DR   Pfam; PF22627; AglB_core-like; 1.
DR   Pfam; PF18079; AglB_L1; 1.
DR   Pfam; PF02516; STT3; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001941};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABD42551.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        370..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..440
FT                   /note="Oligosaccharyl transferase STT3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02516"
FT   DOMAIN          519..619
FT                   /note="AglB-like core"
FT                   /evidence="ECO:0000259|Pfam:PF22627"
FT   DOMAIN          789..854
FT                   /note="Archaeal glycosylation protein B peripheral"
FT                   /evidence="ECO:0000259|Pfam:PF18079"
FT   REGION          450..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  96123 MW;  CBF215D589D26E1A CRC64;
     MEYSRYLKPF TLILGAIVLL ITFFSFIIRT LPAYSGTTDV LMFVGMDDPT YQLRRIEQII
     ANYPNVAWFD PMTYFPIGQP MHWGPLFPFL GATICLITGA ATRTEIISVS LFLPCVMAAL
     MVPVIYLLVS RVADWKAGLA AAFFIAIVPG QFFFRSFYGY LDHHAGEVFF STLFCLCYLT
     ALVYSRKHPV DLKDKETWKI PIFLGILCGI TYVLGLALMP TMLLFALIVG IFTPVWFIIQ
     RYIGHLGASA LVINSVTFLV AIIGFFFIGV HSEGGLNYYT IGHPIAYTLL ILANVLLFGF
     SYQLRDKPYW YYVGAIIGVT ILGIIALAVI LPDLFAYMMA NANAFFGSDD IHWKTIQEAR
     PWSFDDAWRT FQYSLLLFGA GAAVLLYRIR KELCPSHAFT LIWAVVIFYA TCQHIRYEYY
     LAVPVAILAG IAVGFALDII RLPFGQKPEI SPMDEDHQSG KKKAGKSHDV SRGRSGHPAG
     SVKAGSYLFL AIILILALLF SYQALGRDLM MGAYNLNPDW REATEWMNKN TPDPGVDYFA
     MYDEKNFTYP DSAYGVMSWW DYGHMITFLG KRMPNANPFQ YGVNGPNGSA RFFMTKNESE
     ADQILANLKT KYVITDYEMD TGKFWAMSTW DDPEVGVYPY QRTFIFPSPD DPKSGVNYPL
     LTNEYYQTMI SRLHNFDGTY TEPGNVYFLR YMKPSATGLN APVVVDGGQT NYSAGKALVN
     SFNAQENPQY DVILANFGYT DPVEPVPALS HYRLIFESST RTTPADMHDL RYVKIFEHVK
     GAQIPGEGML ELPVKTNTGR EFIYRTQSIN GTFTVPYPTE TTVGAVTIPG KYRNTKNGAE
     YQVTEKQVIE GQSI
//