PGLB_CAMJR
ID PGLB_CAMJR Reviewed; 713 AA.
AC Q5HTX9;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Undecaprenyl-diphosphooligosaccharide--protein glycotransferase;
DE EC=2.4.99.19 {ECO:0000269|PubMed:20007322};
DE AltName: Full=Protein glycosylation B;
GN Name=pglB; OrderedLocusNames=CJE1268;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
RN [2]
RP DOMAIN.
RX PubMed=21812456; DOI=10.1021/bi201018d;
RA Jaffee M.B., Imperiali B.;
RT "Exploiting topological constraints to reveal buried sequence motifs in the
RT membrane-bound N-linked oligosaccharyl transferases.";
RL Biochemistry 50:7557-7567(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 428-713, FUNCTION, AND
RP MUTAGENESIS OF SER-52; ASN-53; ASP-54; MET-568; SER-569; LEU-570 AND
RP ILE-571.
RC STRAIN=RM1221;
RX PubMed=20007322; DOI=10.1074/jbc.m109.081752;
RA Maita N., Nyirenda J., Igura M., Kamishikiryo J., Kohda D.;
RT "Comparative structural biology of eubacterial and archaeal
RT oligosaccharyltransferases.";
RL J. Biol. Chem. 285:4941-4950(2010).
CC -!- FUNCTION: Oligosaccharyltransferase that catalyzes the transfer of a
CC preassembled heptasaccharide from a lipid donor to an asparagine
CC residue in nascent polypeptide chains, affording a beta-linked glycan
CC to the asparagine side chain of target proteins.
CC {ECO:0000269|PubMed:20007322}.
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in
CC eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the
CC lipid carrier undecaprenol-pyrophosphate to an asparagine residue
CC within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide
CC chains, the first step in protein N-glycosylation.
CC {ECO:0000250|UniProtKB:B9KDD4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tritrans,heptacis-undecaprenyl diphosphooligosaccharide +
CC [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate +
CC a glycoprotein with the oligosaccharide chain attached by N-beta-D-
CC glycosyl linkage to protein L-asparagine.; EC=2.4.99.19;
CC Evidence={ECO:0000269|PubMed:20007322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:B9KDD4}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:B9KDD4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:B9KDD4}.
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:B9KDD4}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; CP000025; AAW35590.1; -; Genomic_DNA.
DR RefSeq; WP_011049884.1; NC_003912.7.
DR PDB; 3AAG; X-ray; 2.80 A; A/B=428-713.
DR PDBsum; 3AAG; -.
DR AlphaFoldDB; Q5HTX9; -.
DR SMR; Q5HTX9; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR KEGG; cjr:CJE1268; -.
DR HOGENOM; CLU_024679_0_0_7; -.
DR OMA; GYPIRYY; -.
DR BRENDA; 2.4.99.18; 1087.
DR BRENDA; 2.4.99.19; 1087.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q5HTX9; -.
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; IMP:TIGR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:TIGR.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR041563; STT3_PglB_C.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
DR Pfam; PF18527; STT3_PglB_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Glycoprotein;
KW Glycosyltransferase; Magnesium; Manganese; Membrane; Metal-binding;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..713
FT /note="Undecaprenyl-diphosphooligosaccharide--protein
FT glycotransferase"
FT /id="PRO_0000422588"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 36..96
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..122
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 123..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 145..152
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 175..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..192
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 193..197
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..215
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 216..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..233
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 234..237
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..254
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 255..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 261..278
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 279..324
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 348..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..369
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 370..373
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 397..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT TOPO_DOM 428..713
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT REGION 457..459
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 52..54
FT /note="DXD motif 1"
FT /evidence="ECO:0000305|PubMed:21812456"
FT MOTIF 152..154
FT /note="DXD motif 2"
FT /evidence="ECO:0000305|PubMed:21812456"
FT MOTIF 313..316
FT /note="TIXE motif"
FT /evidence="ECO:0000305|PubMed:21812456"
FT MOTIF 457..461
FT /note="WWDYG motif"
FT /evidence="ECO:0000305|PubMed:21812456"
FT MOTIF 568..575
FT /note="MI motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT BINDING 54
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 194..196
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 291
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 316
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 372
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 462
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 54
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 145
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 316
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 328
FT /note="Interacts with target acceptor peptide in protein
FT substrate; important for extended sequon recognition"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 571
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 534
FT /note="N-linked (DATDGlc) asparagine"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MUTAGEN 52
FT /note="S->E,D: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT MUTAGEN 53
FT /note="N->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT MUTAGEN 54
FT /note="D->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT MUTAGEN 568
FT /note="M->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT MUTAGEN 569
FT /note="S->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT MUTAGEN 570
FT /note="L->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT MUTAGEN 571
FT /note="I->A: Strong reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:20007322"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 495..510
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 525..531
FT /evidence="ECO:0007829|PDB:3AAG"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 538..544
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 560..565
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 566..570
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 572..577
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 594..597
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:3AAG"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 632..639
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 644..649
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:3AAG"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:3AAG"
FT HELIX 682..686
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:3AAG"
FT STRAND 704..712
FT /evidence="ECO:0007829|PDB:3AAG"
SQ SEQUENCE 713 AA; 82206 MW; B5D4836BF36D8FF8 CRC64;
MLKKEYLKNP YLVLFAMIIL AYVFSVLCRF YWIWWASEFN EYFFNNQLMI ISNDGYAFAE
GARDMIAGFH QPNDLSYYGS SLSTLTYWLY KITPFSFESI ILYMSTFLSS LVVIPIILLA
NEYKRPLMGF VAALLASVAN SYYNRTMSGY YDTDMLVIVL PMFILFFMVR MILKKDFFSL
IALPLFIGIY LWWYPSSYTL NVALIGLFLI YTLIFHRKEK IFYIAVILSS LTLSNIAWFY
QSAIIVILFA LFALEQKRLN FMIIGILGSA TLIFLILSGG VDPILYQLKF YIFRNDESAN
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH KSMIMALPIL
VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY SQLTSNVCIV FATILTLAPV
FIHIYNYKAP TVFSQNEASL LNQLKNIANR EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL
GKDNFFPSFA LSKDEQAAAN MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL
FLASLSKPDF KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI DDKAQFYIFY
LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV INSRDAKVFK LKI
