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Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.19) (Protein glycosylation B)

 PGLB_CAMJR              Reviewed;         713 AA.
Q5HTX9;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
28-FEB-2018, entry version 65.
RecName: Full=Undecaprenyl-diphosphooligosaccharide--protein glycotransferase;
EC=2.4.99.19;
AltName: Full=Protein glycosylation B;
Name=pglB; OrderedLocusNames=CJE1268;
Campylobacter jejuni (strain RM1221).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=195099;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RM1221;
PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms
from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
[2]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 428-713, FUNCTION, AND
MUTAGENESIS OF SER-52; ASN-53; ASP-54; MET-568; SER-569; LEU-570 AND
ILE-571.
STRAIN=RM1221;
PubMed=20007322; DOI=10.1074/jbc.M109.081752;
Maita N., Nyirenda J., Igura M., Kamishikiryo J., Kohda D.;
"Comparative structural biology of eubacterial and archaeal
oligosaccharyltransferases.";
J. Biol. Chem. 285:4941-4950(2010).
-!- FUNCTION: Oligosaccharyltransferase that catalyzes the transfer of
a preassembled heptasaccharide from a lipid donor to an asparagine
residue in nascent polypeptide chains, affording a beta-linked
glycan to the asparagine side chain of target proteins.
{ECO:0000269|PubMed:20007322}.
-!- CATALYTIC ACTIVITY: Tritrans,heptacis-undecaprenyl
diphosphooligosaccharide + [protein]-L-asparagine =
tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with
the oligosaccharide chain attached by N-beta-D-glycosyl linkage to
protein L-asparagine.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-
pass membrane protein {ECO:0000250}.
-!- MISCELLANEOUS: N-linked protein glycosylation in C.jejuni consists
in the transfer of a heptasaccharide (GalNAc-alpha1,4-GalNAc-
alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-
alpha1,3-bacillosamine) from a membrane-anchored
undecaprenylpyrophosphate (Und-PP)-linked donor to the Asn side
chain of proteins at the Asn-X-Ser/Thr motif.
-!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP000025; AAW35590.1; -; Genomic_DNA.
RefSeq; WP_011049884.1; NC_003912.7.
PDB; 3AAG; X-ray; 2.80 A; A/B=428-713.
PDBsum; 3AAG; -.
SMR; Q5HTX9; -.
CAZy; GT66; Glycosyltransferase Family 66.
EnsemblBacteria; AAW35590; AAW35590; CJE1268.
KEGG; cjr:CJE1268; -.
HOGENOM; HOG000103852; -.
KO; K17251; -.
OMA; GYPIRYY; -.
BioCyc; CJEJ195099:G1G43-1269-MONOMER; -.
BRENDA; 2.4.99.18; 1087.
BRENDA; 2.4.99.19; 1087.
UniPathway; UPA00378; -.
EvolutionaryTrace; Q5HTX9; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IMP:TIGR.
GO; GO:0006487; P:protein N-linked glycosylation; IMP:TIGR.
InterPro; IPR003674; Oligo_trans_STT3.
Pfam; PF02516; STT3; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Glycosyltransferase;
Magnesium; Membrane; Metal-binding; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 713 Undecaprenyl-diphosphooligosaccharide--
protein glycotransferase.
/FTId=PRO_0000422588.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical. {ECO:0000255}.
TOPO_DOM 34 99 Periplasmic. {ECO:0000255}.
TRANSMEM 100 120 Helical. {ECO:0000255}.
TOPO_DOM 121 125 Cytoplasmic. {ECO:0000255}.
TRANSMEM 126 143 Helical. {ECO:0000255}.
TOPO_DOM 144 176 Periplasmic. {ECO:0000255}.
TRANSMEM 177 193 Helical. {ECO:0000255}.
TOPO_DOM 194 197 Cytoplasmic. {ECO:0000255}.
TRANSMEM 198 218 Helical. {ECO:0000255}.
TOPO_DOM 219 232 Periplasmic. {ECO:0000255}.
TRANSMEM 233 253 Helical. {ECO:0000255}.
TOPO_DOM 254 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical. {ECO:0000255}.
TOPO_DOM 282 328 Periplasmic. {ECO:0000255}.
TRANSMEM 329 349 Helical. {ECO:0000255}.
TOPO_DOM 350 352 Cytoplasmic. {ECO:0000255}.
TRANSMEM 353 373 Helical. {ECO:0000255}.
TOPO_DOM 374 376 Periplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 406 Cytoplasmic. {ECO:0000255}.
TRANSMEM 407 427 Helical. {ECO:0000255}.
TOPO_DOM 428 713 Periplasmic. {ECO:0000255}.
REGION 315 316 Target acceptor peptide binding.
{ECO:0000250}.
ACT_SITE 54 54 {ECO:0000250}.
ACT_SITE 152 152 {ECO:0000250}.
ACT_SITE 316 316 {ECO:0000250}.
METAL 54 54 Magnesium 1. {ECO:0000250}.
METAL 71 71 Magnesium 2. {ECO:0000250}.
METAL 74 74 Magnesium 2. {ECO:0000250}.
METAL 152 152 Magnesium 1. {ECO:0000250}.
METAL 316 316 Magnesium 1. {ECO:0000250}.
METAL 469 469 Magnesium 2. {ECO:0000250}.
BINDING 150 150 Target acceptor peptide. {ECO:0000250}.
BINDING 328 328 Target acceptor peptide. {ECO:0000250}.
BINDING 459 459 Target acceptor peptide. {ECO:0000250}.
MUTAGEN 52 52 S->E,D: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:20007322}.
MUTAGEN 53 53 N->A: Reduced catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 54 54 D->A: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:20007322}.
MUTAGEN 568 568 M->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 569 569 S->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 570 570 L->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 571 571 I->A: Strong reduction in catalytic
activity. {ECO:0000269|PubMed:20007322}.
HELIX 437 444 {ECO:0000244|PDB:3AAG}.
STRAND 453 455 {ECO:0000244|PDB:3AAG}.
HELIX 458 460 {ECO:0000244|PDB:3AAG}.
HELIX 461 468 {ECO:0000244|PDB:3AAG}.
HELIX 481 492 {ECO:0000244|PDB:3AAG}.
HELIX 495 510 {ECO:0000244|PDB:3AAG}.
HELIX 525 531 {ECO:0000244|PDB:3AAG}.
TURN 532 534 {ECO:0000244|PDB:3AAG}.
HELIX 538 544 {ECO:0000244|PDB:3AAG}.
STRAND 560 565 {ECO:0000244|PDB:3AAG}.
HELIX 566 570 {ECO:0000244|PDB:3AAG}.
HELIX 572 577 {ECO:0000244|PDB:3AAG}.
STRAND 594 597 {ECO:0000244|PDB:3AAG}.
STRAND 599 601 {ECO:0000244|PDB:3AAG}.
STRAND 606 609 {ECO:0000244|PDB:3AAG}.
STRAND 614 616 {ECO:0000244|PDB:3AAG}.
TURN 624 626 {ECO:0000244|PDB:3AAG}.
STRAND 632 639 {ECO:0000244|PDB:3AAG}.
STRAND 644 649 {ECO:0000244|PDB:3AAG}.
STRAND 657 660 {ECO:0000244|PDB:3AAG}.
STRAND 670 674 {ECO:0000244|PDB:3AAG}.
TURN 678 680 {ECO:0000244|PDB:3AAG}.
HELIX 682 686 {ECO:0000244|PDB:3AAG}.
STRAND 697 699 {ECO:0000244|PDB:3AAG}.
STRAND 704 712 {ECO:0000244|PDB:3AAG}.
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


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