PGLB_CAMJE
ID PGLB_CAMJE Reviewed; 713 AA.
AC Q0P9C8;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Undecaprenyl-diphosphooligosaccharide--protein glycotransferase;
DE EC=2.4.99.19;
DE AltName: Full=Protein glycosylation B;
GN Name=pglB; OrderedLocusNames=Cj1126c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16356848; DOI=10.1016/j.chembiol.2005.10.004;
RA Glover K.J., Weerapana E., Numao S., Imperiali B.;
RT "Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial
RT oligosaccharyl transferase from Campylobacter jejuni.";
RL Chem. Biol. 12:1311-1315(2005).
RN [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=20331969; DOI=10.1016/j.bbrc.2010.03.126;
RA Li L., Woodward R., Ding Y., Liu X.W., Yi W., Bhatt V.S., Chen M.,
RA Zhang L.W., Wang P.G.;
RT "Overexpression and topology of bacterial oligosaccharyltransferase PglB.";
RL Biochem. Biophys. Res. Commun. 394:1069-1074(2010).
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:0000269|PubMed:16356848}.
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:16356848};
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:0000269|PubMed:16356848}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:20331969}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:20331969}.
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; AL111168; CAL35243.1; -; Genomic_DNA.
DR PIR; A81317; A81317.
DR RefSeq; WP_002852780.1; NC_002163.1.
DR RefSeq; YP_002344519.1; NC_002163.1.
DR AlphaFoldDB; Q0P9C8; -.
DR SMR; Q0P9C8; -.
DR IntAct; Q0P9C8; 1.
DR STRING; 192222.Cj1126c; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR PaxDb; Q0P9C8; -.
DR PRIDE; Q0P9C8; -.
DR EnsemblBacteria; CAL35243; CAL35243; Cj1126c.
DR GeneID; 905417; -.
DR KEGG; cje:Cj1126c; -.
DR PATRIC; fig|192222.6.peg.1108; -.
DR eggNOG; COG1287; Bacteria.
DR HOGENOM; CLU_024679_0_0_7; -.
DR OMA; GYPIRYY; -.
DR BioCyc; MetaCyc:MON-17335; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:8747; -.
DR Proteomes; UP000000799; 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:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
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 Cell inner membrane; Cell membrane; Glycoprotein; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..713
FT /note="Undecaprenyl-diphosphooligosaccharide--protein
FT glycotransferase"
FT /id="PRO_0000422587"
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:0000255"
FT MOTIF 152..154
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 313..316
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 457..461
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
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"
SQ SEQUENCE 713 AA; 82201 MW; 0ACC149A14968DE2 CRC64;
MLKKEYLKNP YLVLFAMIVL AYVFSVFCRF YWVWWASEFN 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 YIFRSDESAN
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH KSMIMALPIL
VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY SQLTSNVCIV FATILTLAPV
FIHIYNYKAP TVFSQNEASL LNQLKNIANR EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL
GKDNFFPSFS LSKDEQAAAN MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL
FLASLSKPDF KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI DDKAQFYIFY
LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV INSRDAKVFK LKI
