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Protein

Undecaprenyl-diphosphooligosaccharide--protein glycotransferase

Gene

pglB

Organism
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
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.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 Publication

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 sitei56 – 5611 Publication
Metal bindingi56 – 561Magnesium 11 Publication
Metal bindingi73 – 731Magnesium 21 Publication
Metal bindingi76 – 761Magnesium 21 Publication
Binding sitei152 – 1521Target acceptor peptide
Active sitei154 – 15411 Publication
Metal bindingi154 – 1541Magnesium 11 Publication
Active sitei319 – 31911 Publication
Metal bindingi319 – 3191Magnesium 11 Publication
Binding sitei331 – 3311Target acceptor peptide
Binding sitei465 – 4651Target acceptor peptide
Metal bindingi475 – 4751Magnesium 21 Publication

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB
  • oligosaccharyl transferase activity Source: InterPro
  • transferase activity, transferring glycosyl groups Source: UniProtKB

GO - Biological processi

  • protein N-linked glycosylation via asparagine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciCLAR306263:GH7X-1251-MONOMER.
BRENDAi2.4.99.19. 13108.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.
TCDBi9.B.142.3.11. the integral membrane glycosyltransferase family 39 (gt39) family.

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:Cla_1253
OrganismiCampylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
Taxonomic identifieri306263 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000007727 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence analysisAdd
BLAST
Transmembranei18 – 3821HelicalSequence analysisAdd
BLAST
Topological domaini39 – 7840PeriplasmicSequence analysisAdd
BLAST
Transmembranei79 – 9921HelicalSequence analysisAdd
BLAST
Topological domaini100 – 1012CytoplasmicSequence analysis
Transmembranei102 – 12221HelicalSequence analysisAdd
BLAST
Topological domaini123 – 1264PeriplasmicSequence analysis
Transmembranei127 – 14620HelicalSequence analysisAdd
BLAST
Topological domaini147 – 1504CytoplasmicSequence analysis
Transmembranei151 – 17121HelicalSequence analysisAdd
BLAST
Topological domaini172 – 1787PeriplasmicSequence analysis
Transmembranei179 – 19921HelicalSequence analysisAdd
BLAST
Topological domaini200 – 2001CytoplasmicSequence analysis
Transmembranei201 – 21717HelicalSequence analysisAdd
BLAST
Topological domaini218 – 23013PeriplasmicSequence analysisAdd
BLAST
Transmembranei231 – 25121HelicalSequence analysisAdd
BLAST
Topological domaini252 – 26211CytoplasmicSequence analysisAdd
BLAST
Transmembranei263 – 28321HelicalSequence analysisAdd
BLAST
Topological domaini284 – 33148PeriplasmicSequence analysisAdd
BLAST
Transmembranei332 – 35221HelicalSequence analysisAdd
BLAST
Topological domaini353 – 3531CytoplasmicSequence analysis
Transmembranei354 – 37421HelicalSequence analysisAdd
BLAST
Topological domaini375 – 3751PeriplasmicSequence analysis
Transmembranei376 – 39621HelicalSequence analysisAdd
BLAST
Topological domaini397 – 41216CytoplasmicSequence analysisAdd
BLAST
Transmembranei413 – 43321HelicalSequence analysisAdd
BLAST
Topological domaini434 – 712279PeriplasmicSequence 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
Mutagenesisi56 – 561D → A: Strongly reduced catalytic activity. Abolished catalytic activity; when associated with A-319. 1 Publication
Mutagenesisi154 – 1541D → A: Reduced catalytic activity. 1 Publication
Mutagenesisi319 – 3191E → A: Strongly reduced catalytic activity. Abolished catalytic activity; when associated with A-56. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 712712Undecaprenyl-diphosphooligosaccharide--protein glycotransferasePRO_0000422589Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-59188N.
STRINGi306263.Cla_1253.

Structurei

Secondary structure

1
712
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 3119Combined sources
Helixi33 – 386Combined sources
Helixi42 – 443Combined sources
Helixi55 – 6915Combined sources
Helixi83 – 9311Combined sources
Helixi99 – 11012Combined sources
Helixi111 – 1144Combined sources
Helixi115 – 12410Combined sources
Helixi128 – 13811Combined sources
Helixi142 – 1465Combined sources
Helixi155 – 1584Combined sources
Helixi161 – 17616Combined sources
Helixi180 – 19415Combined sources
Helixi197 – 1993Combined sources
Helixi200 – 21819Combined sources
Helixi222 – 23514Combined sources
Helixi240 – 25617Combined sources
Helixi263 – 28018Combined sources
Turni313 – 3164Combined sources
Helixi318 – 3203Combined sources
Helixi325 – 3339Combined sources
Helixi336 – 35015Combined sources
Helixi356 – 3594Combined sources
Helixi360 – 37213Combined sources
Helixi374 – 3807Combined sources
Helixi381 – 40121Combined sources
Helixi408 – 43225Combined sources
Helixi441 – 45111Combined sources
Beta strandi459 – 4613Combined sources
Helixi464 – 47411Combined sources
Beta strandi477 – 4793Combined sources
Beta strandi482 – 4843Combined sources
Helixi487 – 49812Combined sources
Helixi501 – 52121Combined sources
Helixi526 – 5327Combined sources
Turni533 – 5353Combined sources
Beta strandi537 – 5393Combined sources
Helixi540 – 5434Combined sources
Beta strandi548 – 5503Combined sources
Beta strandi561 – 5666Combined sources
Helixi567 – 5704Combined sources
Helixi573 – 5819Combined sources
Turni584 – 5863Combined sources
Beta strandi596 – 5983Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi610 – 6123Combined sources
Turni613 – 6153Combined sources
Beta strandi616 – 6194Combined sources
Turni620 – 6234Combined sources
Beta strandi624 – 6296Combined sources
Beta strandi631 – 64212Combined sources
Turni643 – 6464Combined sources
Beta strandi647 – 6526Combined sources
Beta strandi659 – 6646Combined sources
Turni665 – 6684Combined sources
Beta strandi669 – 6746Combined sources
Helixi675 – 6784Combined sources
Helixi681 – 6855Combined sources
Turni693 – 6953Combined sources
Beta strandi698 – 7025Combined sources
Beta strandi705 – 7095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCEX-ray3.40A1-712[»]
ProteinModelPortaliB9KDD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni318 – 3192Target acceptor peptide binding

Sequence similaritiesi

Belongs to the STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107ZAZ. Bacteria.
COG1287. LUCA.
HOGENOMiHOG000103852.
KOiK17251.
OMAiGYPIRYY.
OrthoDBiPOG091H1IN5.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

B9KDD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLQQNFTDN NSIKYTCILI LIAFAFSVLC RLYWVAWASE FYEFFFNDQL
60 70 80 90 100
MITTNDGYAF AEGARDMIAG FHQPNDLSYF GSSLSTLTYW LYSILPFSFE
110 120 130 140 150
SIILYMSAFF ASLIVVPIIL IAREYKLTTY GFIAALLGSI ANSYYNRTMS
160 170 180 190 200
GYYDTDMLVL VLPMLILLTF IRLTINKDIF TLLLSPVFIM IYLWWYPSSY
210 220 230 240 250
SLNFAMIGLF GLYTLVFHRK EKIFYLTIAL MIIALSMLAW QYKLALIVLL
260 270 280 290 300
FAIFAFKEEK INFYMIWALI FISILILHLS GGLDPVLYQL KFYVFKASDV
310 320 330 340 350
QNLKDAAFMY FNVNETIMEV NTIDPEVFMQ RISSSVLVFI LSFIGFILLC
360 370 380 390 400
KDHKSMLLAL PMLALGFMAL RAGLRFTIYA VPVMALGFGY FLYAFFNFLE
410 420 430 440 450
KKQIKLSLRN KNILLILIAF FSISPALMHI YYYKSSTVFT SYEASILNDL
460 470 480 490 500
KNKAQREDYV VAWWDYGYPI RYYSDVKTLI DGGKHLGKDN FFSSFVLSKE
510 520 530 540 550
QIPAANMARL SVEYTEKSFK ENYPDVLKAM VKDYNKTSAK DFLESLNDKD
560 570 580 590 600
FKFDTNKTRD VYIYMPYRML RIMPVVAQFA NTNPDNGEQE KSLFFSQANA
610 620 630 640 650
IAQDKTTGSV MLDNGVEIIN DFRALKVEGA SIPLKAFVDI ESITNGKFYY
660 670 680 690 700
NEIDSKAQIY LLFLREYKSF VILDESLYNS SYIQMFLLNQ YDQDLFEQIT
710
NDTRAKIYRL KR
Length:712
Mass (Da):82,729
Last modified:March 24, 2009 - v1
Checksum:iA04C959507F3C581
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000932 Genomic DNA. Translation: ACM64573.1.
RefSeqiWP_012661956.1. NC_012039.1.

Genome annotation databases

EnsemblBacteriaiACM64573; ACM64573; Cla_1253.
GeneIDi7410986.
KEGGicla:Cla_1253.
PATRICi20062993. VBICamLar15090_1240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000932 Genomic DNA. Translation: ACM64573.1.
RefSeqiWP_012661956.1. NC_012039.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCEX-ray3.40A1-712[»]
ProteinModelPortaliB9KDD4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59188N.
STRINGi306263.Cla_1253.

Protein family/group databases

CAZyiGT66. Glycosyltransferase Family 66.
TCDBi9.B.142.3.11. the integral membrane glycosyltransferase family 39 (gt39) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM64573; ACM64573; Cla_1253.
GeneIDi7410986.
KEGGicla:Cla_1253.
PATRICi20062993. VBICamLar15090_1240.

Phylogenomic databases

eggNOGiENOG4107ZAZ. Bacteria.
COG1287. LUCA.
HOGENOMiHOG000103852.
KOiK17251.
OMAiGYPIRYY.
OrthoDBiPOG091H1IN5.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciCLAR306263:GH7X-1251-MONOMER.
BRENDAi2.4.99.19. 13108.

Family and domain databases

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

Entry informationi

Entry nameiPGLB_CAMLR
AccessioniPrimary (citable) accession number: B9KDD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: March 24, 2009
Last modified: September 7, 2016
This is version 45 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.lari 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, Complete proteome, Reference proteome

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.