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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)DescriptionActionsGraphical viewLength
Active sitei54By similarity1
Metal bindingi54Magnesium 1By similarity1
Metal bindingi71Magnesium 2By similarity1
Metal bindingi74Magnesium 2By similarity1
Binding sitei150Target acceptor peptideBy similarity1
Active sitei152By similarity1
Metal bindingi152Magnesium 1By similarity1
Active sitei316By similarity1
Metal bindingi316Magnesium 1By similarity1
Binding sitei328Target acceptor peptideBy similarity1
Binding sitei459Target acceptor peptideBy similarity1
Metal bindingi469Magnesium 2By similarity1

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

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 33HelicalSequence analysisAdd BLAST21
Topological domaini34 – 99PeriplasmicSequence analysisAdd BLAST66
Transmembranei100 – 120HelicalSequence analysisAdd BLAST21
Topological domaini121 – 125CytoplasmicSequence analysis5
Transmembranei126 – 143HelicalSequence analysisAdd BLAST18
Topological domaini144 – 176PeriplasmicSequence analysisAdd BLAST33
Transmembranei177 – 193HelicalSequence analysisAdd BLAST17
Topological domaini194 – 197CytoplasmicSequence analysis4
Transmembranei198 – 218HelicalSequence analysisAdd BLAST21
Topological domaini219 – 232PeriplasmicSequence analysisAdd BLAST14
Transmembranei233 – 253HelicalSequence analysisAdd BLAST21
Topological domaini254 – 260CytoplasmicSequence analysis7
Transmembranei261 – 281HelicalSequence analysisAdd BLAST21
Topological domaini282 – 328PeriplasmicSequence analysisAdd BLAST47
Transmembranei329 – 349HelicalSequence analysisAdd BLAST21
Topological domaini350 – 352CytoplasmicSequence analysis3
Transmembranei353 – 373HelicalSequence analysisAdd BLAST21
Topological domaini374 – 376PeriplasmicSequence analysis3
Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 406CytoplasmicSequence analysis9
Transmembranei407 – 427HelicalSequence analysisAdd BLAST21
Topological domaini428 – 713PeriplasmicSequence analysisAdd BLAST286

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52S → E or D: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi53N → A: Reduced catalytic activity. 1 Publication1
Mutagenesisi54D → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi568M → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi569S → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi570L → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi571I → A: Strong reduction in catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004225881 – 713Undecaprenyl-diphosphooligosaccharide--protein glycotransferaseAdd BLAST713

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi437 – 447Combined sources11
Beta strandi453 – 455Combined sources3
Helixi458 – 460Combined sources3
Helixi461 – 468Combined sources8
Beta strandi471 – 473Combined sources3
Helixi481 – 492Combined sources12
Helixi495 – 511Combined sources17
Helixi525 – 531Combined sources7
Turni532 – 534Combined sources3
Helixi538 – 544Combined sources7
Beta strandi560 – 565Combined sources6
Helixi566 – 570Combined sources5
Helixi572 – 577Combined sources6
Beta strandi594 – 597Combined sources4
Beta strandi599 – 601Combined sources3
Beta strandi606 – 609Combined sources4
Beta strandi614 – 616Combined sources3
Turni624 – 626Combined sources3
Beta strandi632 – 639Combined sources8
Turni640 – 643Combined sources4
Beta strandi644 – 649Combined sources6
Beta strandi657 – 660Combined sources4
Beta strandi670 – 674Combined sources5
Helixi676 – 680Combined sources5
Helixi682 – 686Combined sources5
Turni694 – 696Combined sources3
Beta strandi697 – 702Combined sources6
Beta strandi704 – 711Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AAGX-ray2.80A/B428-713[»]
SMRiQ5HTX9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5HTX9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni315 – 316Target acceptor peptide bindingBy similarity2

Sequence similaritiesi

Belongs to the STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000103852.
KOiK17251.
OMAiGYPIRYY.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AAGX-ray2.80A/B428-713[»]
SMRiQ5HTX9.
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.

Enzyme and pathway databases

UniPathwayiUPA00378.
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...

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 2, 2016
This is version 62 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.