ID M0CKC9_9EURY Unreviewed; 987 AA.
AC M0CKC9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=C475_15533 {ECO:0000313|EMBL:ELZ23696.1};
OS Halosimplex carlsbadense 2-9-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halosimplex.
OX NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ23696.1, ECO:0000313|Proteomes:UP000011626};
RN [1] {ECO:0000313|EMBL:ELZ23696.1, ECO:0000313|Proteomes:UP000011626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ23696.1,
RC ECO:0000313|Proteomes:UP000011626};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the STT3 family.
CC {ECO:0000256|ARBA:ARBA00010810}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ23696.1}.
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DR EMBL; AOIU01000033; ELZ23696.1; -; Genomic_DNA.
DR RefSeq; WP_006884775.1; NZ_AOIU01000033.1.
DR AlphaFoldDB; M0CKC9; -.
DR STRING; 797114.C475_15533; -.
DR PATRIC; fig|797114.5.peg.3156; -.
DR eggNOG; arCOG02043; Archaea.
DR eggNOG; arCOG07813; Archaea.
DR OrthoDB; 313284at2157; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000011626; Unassembled WGS sequence.
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 Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR048307; STT3_N.
DR PANTHER; PTHR13872; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT; 1.
DR PANTHER; PTHR13872:SF1; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT STT3B; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF02516; STT3; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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:UP000011626};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 849..980
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
SQ SEQUENCE 987 AA; 107041 MW; C7B829442BE6D326 CRC64;
MADARTETEA LLADKSHLES QLEEVLAVDE STESWAFDDV SLDSGAFGEL VSRGIVEEVN
GEYTLADPKA VRQALDGDGS VSSDDEQSAS FTESLSVEFD RVAVAGLLGA LALVVVFRVL
PLQSVFRGGD VVLSGNDPYY YRYLVHELLA VSSNPFDLSV LSSLPSGVAH GEPLMLVSMW
WVSALLGGES AVDGVLAWFP VVSAVVTALL VYALTVRVTD DKRVGIAAVA LLAVTPGHAF
RTGLGFADHH AFDYPWLALT VLAAVSVVGR DILERRTWAW VGALAVGVAG QMLAWDAGPL
LLVPLGLFAL GLVPSVLRDG GSPLRAGRPL LAGVSMGTFV AVLAHISLGW HTPAVIVAPV
LLSVGIAGLL VLGEGARRAE VSSRLVVGVS VVGLVLGIVA LWSLVPVFAT ELERGMDFLL
TTEGIAETTS IVSGDLGTII GPIFLFGFGL FLALGHMCWA LWMSYRRHAP AWLLITVYGW
YFLLLSAIQV RFAGQLALFA ALFGGLGFVH LAAWVDLASV PTPFVDNRLA DGPRVVGSSG
DEFSSAGELV RPNRRQLLHL GVLGFGAGSL GGLLTPIRHS QLVIDDSMYE AAKFMREHSK
EQGWDYPKNY VFSQWGRNRV YNWFVNGESR GYGYAQSNFQ DFVTSGNSAE WYEQLRNRAG
FITIEESDPS ATTEFGELYD QLWSDTFGID TENYRAVWMN STDSLRVFTP VSGALVTGPA
PKNRTLNIEV TAEIGQKSQS IAIERHTGDQ GIYQAVVPLP GIYQVNGNRL SVSEDDVQQG
SVISGFSGNG YAYWSFNEGS GEWAYDRVGG HHGRIHEAEW TNRGRSEFAL SFSGKNSSDF
VESPVTSLQT FTISLWAKPA ALDVSEDNDF RDIIRTPTGR IMVFEQSGKI SFRLPGVDDG
RLTGRGIQTN EWQHIAMTYD GSVRTIYINN ERKARDRVSV GKLDWGGTLR LGNQFSTPSG
HGYAGLLDEV RIHNRVLSDE ELTNLRK
//
