Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei561 Publication1
Metal bindingi56Magnesium 11 Publication1
Metal bindingi73Magnesium 21 Publication1
Metal bindingi76Magnesium 21 Publication1
Binding sitei152Target acceptor peptide1
Active sitei1541 Publication1
Metal bindingi154Magnesium 11 Publication1
Active sitei3191 Publication1
Metal bindingi319Magnesium 11 Publication1
Binding sitei331Target acceptor peptide1
Binding sitei465Target acceptor peptide1
Metal bindingi475Magnesium 21 Publication1

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

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 17CytoplasmicSequence analysisAdd BLAST17
Transmembranei18 – 38HelicalSequence analysisAdd BLAST21
Topological domaini39 – 78PeriplasmicSequence analysisAdd BLAST40
Transmembranei79 – 99HelicalSequence analysisAdd BLAST21
Topological domaini100 – 101CytoplasmicSequence analysis2
Transmembranei102 – 122HelicalSequence analysisAdd BLAST21
Topological domaini123 – 126PeriplasmicSequence analysis4
Transmembranei127 – 146HelicalSequence analysisAdd BLAST20
Topological domaini147 – 150CytoplasmicSequence analysis4
Transmembranei151 – 171HelicalSequence analysisAdd BLAST21
Topological domaini172 – 178PeriplasmicSequence analysis7
Transmembranei179 – 199HelicalSequence analysisAdd BLAST21
Topological domaini200CytoplasmicSequence analysis1
Transmembranei201 – 217HelicalSequence analysisAdd BLAST17
Topological domaini218 – 230PeriplasmicSequence analysisAdd BLAST13
Transmembranei231 – 251HelicalSequence analysisAdd BLAST21
Topological domaini252 – 262CytoplasmicSequence analysisAdd BLAST11
Transmembranei263 – 283HelicalSequence analysisAdd BLAST21
Topological domaini284 – 331PeriplasmicSequence analysisAdd BLAST48
Transmembranei332 – 352HelicalSequence analysisAdd BLAST21
Topological domaini353CytoplasmicSequence analysis1
Transmembranei354 – 374HelicalSequence analysisAdd BLAST21
Topological domaini375PeriplasmicSequence analysis1
Transmembranei376 – 396HelicalSequence analysisAdd BLAST21
Topological domaini397 – 412CytoplasmicSequence analysisAdd BLAST16
Transmembranei413 – 433HelicalSequence analysisAdd BLAST21
Topological domaini434 – 712PeriplasmicSequence analysisAdd BLAST279

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi56D → A: Strongly reduced catalytic activity. Abolished catalytic activity; when associated with A-319. 1 Publication1
Mutagenesisi154D → A: Reduced catalytic activity. 1 Publication1
Mutagenesisi319E → A: Strongly reduced catalytic activity. Abolished catalytic activity; when associated with A-56. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004225891 – 712Undecaprenyl-diphosphooligosaccharide--protein glycotransferaseAdd BLAST712

Interactioni

Protein-protein interaction databases

DIPiDIP-59188N.
STRINGi306263.Cla_1253.

Structurei

Secondary structure

1712
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 31Combined sources19
Helixi33 – 38Combined sources6
Helixi42 – 44Combined sources3
Helixi55 – 69Combined sources15
Helixi83 – 93Combined sources11
Helixi99 – 110Combined sources12
Helixi111 – 114Combined sources4
Helixi115 – 124Combined sources10
Helixi128 – 138Combined sources11
Helixi142 – 146Combined sources5
Helixi155 – 158Combined sources4
Helixi161 – 176Combined sources16
Helixi180 – 194Combined sources15
Helixi197 – 199Combined sources3
Helixi200 – 218Combined sources19
Helixi222 – 235Combined sources14
Helixi240 – 256Combined sources17
Helixi263 – 280Combined sources18
Turni313 – 316Combined sources4
Helixi318 – 320Combined sources3
Helixi325 – 333Combined sources9
Helixi336 – 350Combined sources15
Helixi356 – 359Combined sources4
Helixi360 – 372Combined sources13
Helixi374 – 380Combined sources7
Helixi381 – 401Combined sources21
Helixi408 – 432Combined sources25
Helixi441 – 451Combined sources11
Beta strandi459 – 461Combined sources3
Helixi464 – 474Combined sources11
Beta strandi477 – 479Combined sources3
Beta strandi482 – 484Combined sources3
Helixi487 – 498Combined sources12
Helixi501 – 521Combined sources21
Helixi526 – 532Combined sources7
Turni533 – 535Combined sources3
Beta strandi537 – 539Combined sources3
Helixi540 – 543Combined sources4
Beta strandi548 – 550Combined sources3
Beta strandi561 – 566Combined sources6
Helixi567 – 570Combined sources4
Helixi573 – 581Combined sources9
Turni584 – 586Combined sources3
Beta strandi596 – 598Combined sources3
Beta strandi600 – 602Combined sources3
Beta strandi610 – 612Combined sources3
Turni613 – 615Combined sources3
Beta strandi616 – 619Combined sources4
Turni620 – 623Combined sources4
Beta strandi624 – 629Combined sources6
Beta strandi631 – 642Combined sources12
Turni643 – 646Combined sources4
Beta strandi647 – 652Combined sources6
Beta strandi659 – 664Combined sources6
Turni665 – 668Combined sources4
Beta strandi669 – 674Combined sources6
Helixi675 – 678Combined sources4
Helixi681 – 685Combined sources5
Turni693 – 695Combined sources3
Beta strandi698 – 702Combined sources5
Beta strandi705 – 709Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RCEX-ray3.40A1-712[»]
ProteinModelPortaliB9KDD4.
SMRiB9KDD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni318 – 319Target acceptor peptide binding2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RCEX-ray3.40A1-712[»]
ProteinModelPortaliB9KDD4.
SMRiB9KDD4.
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.
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: November 2, 2016
This is version 46 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.