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Protein

Undecaprenyl-diphosphooligosaccharide--protein glycotransferase

Gene

pglB

Organism
Campylobacter jejuni (strain RM1221)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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.

Cofactori

Mg2+By similarity, Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541By similarity
Metal bindingi54 – 541Magnesium 1By similarity
Metal bindingi71 – 711Magnesium 2By similarity
Metal bindingi74 – 741Magnesium 2By similarity
Binding sitei150 – 1501Target acceptor peptideBy similarity
Active sitei152 – 1521By similarity
Metal bindingi152 – 1521Magnesium 1By similarity
Active sitei316 – 3161By similarity
Metal bindingi316 – 3161Magnesium 1By similarity
Binding sitei328 – 3281Target acceptor peptideBy similarity
Binding sitei459 – 4591Target acceptor peptideBy similarity
Metal bindingi469 – 4691Magnesium 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • oligosaccharyl transferase activity Source: InterPro
  • transferase activity, transferring glycosyl groups Source: TIGR

GO - Biological processi

  • protein N-linked glycosylation Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCJEJ195099:GJC0-1294-MONOMER.
BRENDAi2.4.99.18. 1087.
2.4.99.19. 1087.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.

Names & Taxonomyi

Protein namesi
Recommended name:
Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC:2.4.99.19)
Alternative name(s):
Protein glycosylation B
Gene namesi
Name:pglB
Ordered Locus Names:CJE1268
OrganismiCampylobacter jejuni (strain RM1221)
Taxonomic identifieri195099 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3321HelicalSequence analysisAdd
BLAST
Topological domaini34 – 9966PeriplasmicSequence analysisAdd
BLAST
Transmembranei100 – 12021HelicalSequence analysisAdd
BLAST
Topological domaini121 – 1255CytoplasmicSequence analysis
Transmembranei126 – 14318HelicalSequence analysisAdd
BLAST
Topological domaini144 – 17633PeriplasmicSequence analysisAdd
BLAST
Transmembranei177 – 19317HelicalSequence analysisAdd
BLAST
Topological domaini194 – 1974CytoplasmicSequence analysis
Transmembranei198 – 21821HelicalSequence analysisAdd
BLAST
Topological domaini219 – 23214PeriplasmicSequence analysisAdd
BLAST
Transmembranei233 – 25321HelicalSequence analysisAdd
BLAST
Topological domaini254 – 2607CytoplasmicSequence analysis
Transmembranei261 – 28121HelicalSequence analysisAdd
BLAST
Topological domaini282 – 32847PeriplasmicSequence analysisAdd
BLAST
Transmembranei329 – 34921HelicalSequence analysisAdd
BLAST
Topological domaini350 – 3523CytoplasmicSequence analysis
Transmembranei353 – 37321HelicalSequence analysisAdd
BLAST
Topological domaini374 – 3763PeriplasmicSequence analysis
Transmembranei377 – 39721HelicalSequence analysisAdd
BLAST
Topological domaini398 – 4069CytoplasmicSequence analysis
Transmembranei407 – 42721HelicalSequence analysisAdd
BLAST
Topological domaini428 – 713286PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521S → E or D: Strongly reduced catalytic activity. 1 Publication
Mutagenesisi53 – 531N → A: Reduced catalytic activity. 1 Publication
Mutagenesisi54 – 541D → A: Strongly reduced catalytic activity. 1 Publication
Mutagenesisi568 – 5681M → A: No effect on catalytic activity. 1 Publication
Mutagenesisi569 – 5691S → A: No effect on catalytic activity. 1 Publication
Mutagenesisi570 – 5701L → A: No effect on catalytic activity. 1 Publication
Mutagenesisi571 – 5711I → A: Strong reduction in catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Undecaprenyl-diphosphooligosaccharide--protein glycotransferasePRO_0000422588Add
BLAST

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi437 – 44711Combined sources
Beta strandi453 – 4553Combined sources
Helixi458 – 4603Combined sources
Helixi461 – 4688Combined sources
Beta strandi471 – 4733Combined sources
Helixi481 – 49212Combined sources
Helixi495 – 51117Combined sources
Helixi525 – 5317Combined sources
Turni532 – 5343Combined sources
Helixi538 – 5447Combined sources
Beta strandi560 – 5656Combined sources
Helixi566 – 5705Combined sources
Helixi572 – 5776Combined sources
Beta strandi594 – 5974Combined sources
Beta strandi599 – 6013Combined sources
Beta strandi606 – 6094Combined sources
Beta strandi614 – 6163Combined sources
Turni624 – 6263Combined sources
Beta strandi632 – 6398Combined sources
Turni640 – 6434Combined sources
Beta strandi644 – 6496Combined sources
Beta strandi657 – 6604Combined sources
Beta strandi670 – 6745Combined sources
Helixi676 – 6805Combined sources
Helixi682 – 6865Combined sources
Turni694 – 6963Combined sources
Beta strandi697 – 7026Combined sources
Beta strandi704 – 7118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AAGX-ray2.80A/B428-713[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5HTX9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni315 – 3162Target acceptor peptide bindingBy similarity

Sequence similaritiesi

Belongs to the STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000103852.
KOiK17251.
OMAiGYPIRYY.
OrthoDBiEOG628F1V.

Family and domain databases

InterProiIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamiPF02516. STT3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5HTX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKEYLKNP YLVLFAMIIL AYVFSVLCRF YWIWWASEFN EYFFNNQLMI
60 70 80 90 100
ISNDGYAFAE GARDMIAGFH QPNDLSYYGS SLSTLTYWLY KITPFSFESI
110 120 130 140 150
ILYMSTFLSS LVVIPIILLA NEYKRPLMGF VAALLASVAN SYYNRTMSGY
160 170 180 190 200
YDTDMLVIVL PMFILFFMVR MILKKDFFSL IALPLFIGIY LWWYPSSYTL
210 220 230 240 250
NVALIGLFLI YTLIFHRKEK IFYIAVILSS LTLSNIAWFY QSAIIVILFA
260 270 280 290 300
LFALEQKRLN FMIIGILGSA TLIFLILSGG VDPILYQLKF YIFRNDESAN
310 320 330 340 350
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH
360 370 380 390 400
KSMIMALPIL VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY
410 420 430 440 450
SQLTSNVCIV FATILTLAPV FIHIYNYKAP TVFSQNEASL LNQLKNIANR
460 470 480 490 500
EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL GKDNFFPSFA LSKDEQAAAN
510 520 530 540 550
MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL FLASLSKPDF
560 570 580 590 600
KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL
610 620 630 640 650
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI
660 670 680 690 700
DDKAQFYIFY LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV
710
INSRDAKVFK LKI
Length:713
Mass (Da):82,206
Last modified:February 15, 2005 - v1
Checksum:iB5D4836BF36D8FF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000025 Genomic DNA. Translation: AAW35590.1.
RefSeqiWP_011049884.1. NC_003912.7.

Genome annotation databases

EnsemblBacteriaiAAW35590; AAW35590; CJE1268.
KEGGicjr:CJE1268.
PATRICi20044332. VBICamJej134361_1284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000025 Genomic DNA. Translation: AAW35590.1.
RefSeqiWP_011049884.1. NC_003912.7.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AAGX-ray2.80A/B428-713[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW35590; AAW35590; CJE1268.
KEGGicjr:CJE1268.
PATRICi20044332. VBICamJej134361_1284.

Phylogenomic databases

HOGENOMiHOG000103852.
KOiK17251.
OMAiGYPIRYY.
OrthoDBiEOG628F1V.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciCJEJ195099:GJC0-1294-MONOMER.
BRENDAi2.4.99.18. 1087.
2.4.99.19. 1087.

Miscellaneous databases

EvolutionaryTraceiQ5HTX9.

Family and domain databases

InterProiIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamiPF02516. STT3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RM1221.
  2. "Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases."
    Maita N., Nyirenda J., Igura M., Kamishikiryo J., Kohda D.
    J. Biol. Chem. 285:4941-4950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 428-713, FUNCTION, MUTAGENESIS OF SER-52; ASN-53; ASP-54; MET-568; SER-569; LEU-570 AND ILE-571.
    Strain: RM1221.

Entry informationi

Entry nameiPGLB_CAMJR
AccessioniPrimary (citable) accession number: Q5HTX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: February 15, 2005
Last modified: November 11, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.