General glycosylation pathway protein - Campylobacter jejuni (strain RM1221)

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Q5HTX9 (Q5HTX9_CAMJR) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 44. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
General glycosylation pathway protein EMBL AAW35590.1

Gene names

Name:	pglB EMBL AAW35590.1
Ordered Locus Names:	CJE1268

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP] EMBL AAW35590.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter ›

Protein attributes

Sequence length	713 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 3AAG Metal-binding PDB 3AAG
Technical term	3D-structure PDB 3AAG Complete proteome
Gene Ontology (GO)
Biological_process	protein N-linked glycosylation Inferred from mutant phenotype Ref.1. Source: TIGR
Cellular_component	membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyl transferase activity Inferred from electronic annotation. Source: InterPro transferase activity, transferring glycosyl groups Inferred from mutant phenotype Ref.1. Source: TIGR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

1

Calcium PDB 3AAG

Metal binding

1

Calcium; via carbonyl oxygen PDB 3AAG

Sequences

Sequence

Length

Mass (Da)

Tools

Q5HTX9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B5D4836BF36D8FF8
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713

82,206

        10         20         30         40         50         60 
MLKKEYLKNP YLVLFAMIIL AYVFSVLCRF YWIWWASEFN EYFFNNQLMI ISNDGYAFAE 

        70         80         90        100        110        120 
GARDMIAGFH QPNDLSYYGS SLSTLTYWLY KITPFSFESI ILYMSTFLSS LVVIPIILLA 

       130        140        150        160        170        180 
NEYKRPLMGF VAALLASVAN SYYNRTMSGY YDTDMLVIVL PMFILFFMVR MILKKDFFSL 

       190        200        210        220        230        240 
IALPLFIGIY LWWYPSSYTL NVALIGLFLI YTLIFHRKEK IFYIAVILSS LTLSNIAWFY 

       250        260        270        280        290        300 
QSAIIVILFA LFALEQKRLN FMIIGILGSA TLIFLILSGG VDPILYQLKF YIFRNDESAN 

       310        320        330        340        350        360 
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH KSMIMALPIL 

       370        380        390        400        410        420 
VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY SQLTSNVCIV FATILTLAPV 

       430        440        450        460        470        480 
FIHIYNYKAP TVFSQNEASL LNQLKNIANR EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL 

       490        500        510        520        530        540 
GKDNFFPSFA LSKDEQAAAN MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL 

       550        560        570        580        590        600 
FLASLSKPDF KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL 

       610        620        630        640        650        660 
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI DDKAQFYIFY 

       670        680        690        700        710 
LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV INSRDAKVFK LKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." 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. PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract] 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 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000025 Genomic DNA. Translation: AAW35590.1.

RefSeq

YP_179256.1. NC_003912.7.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AAG	X-ray	2.80	A/B	428-713	[»]

ModBase

Protein-protein interaction databases

STRING

195099.CJE1268.

Protein family/group databases

CAZy

GT66. Glycosyltransferase Family 66.

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

EnsemblBacteria

AAW35590; AAW35590; CJE1268.

GeneID

KEGG

PATRIC

20044332. VBICamJej134361_1284.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

KO

OMA

ProtClustDB

Enzyme and pathway databases

BioCyc

CJEJ195099:GJC0-1294-MONOMER.

Family and domain databases

InterPro

IPR003674. Oligo_trans_STT3.
[Graphical view]

Pfam

PF02516. STT3. 1 hit.
[Graphical view]

ProtoNet

Other

EvolutionaryTrace

Entry information

Entry name

Q5HTX9_CAMJR

Accession

Primary (citable) accession number: Q5HTX9

Entry history

Integrated into UniProtKB/TrEMBL:	February 15, 2005
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info