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Reviewed, UniProtKB/Swiss-Prot Q9PIK8 (LPXB_CAMJE)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lipid-A-disaccharide synthase
    EC=2.4.1.182
Gene names
Name: lpxB
Ordered Locus Names: Cj0288c
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity.

Catalytic activity

UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. HAMAP MF_00392

Pathway

Glycolipid biosynthesis; lipid (IV)A biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-D-glucosamine: step 5/6. HAMAP MF_00392

Sequence similarities

Belongs to the lpxB family.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid synthesis
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid A biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionlipid-A-disaccharide synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Lipid-A-disaccharide synthase HAMAP MF_00392
PRO_0000190156

Sequences

Sequence LengthMass (Da)Tools
Q9PIK8-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 53DA0DA1979A2C5F

FASTA36441,581
        10         20         30         40         50         60 
MKTFLVCALE PSANLHLKEV LKAYKKDFGE FELHGIYDES LCKEFDLNSK PLYSSHEFSA 

        70         80         90        100        110        120 
MGFIEVLPLI FKAKKAIKEL ANLSFTQKIN GILCIDSPAF NIPFAKALKK AGSKIPRIYY 

       130        140        150        160        170        180 
ILPQVWAWKK GRIPIIESHF DILASILPFD NQFFNKSTYI GHPLLDEIKE FKNQEDINHT 

       190        200        210        220        230        240 
FSKKDDEKTI AFLPGSRRSE IRRLMPIFKE LSQKFKGKKI LCVPSFNLEK LEVYGDISEF 

       250        260        270        280        290        300 
KIESNTPKVL KKADFAFICS GTATLEAALV GTPFVLAYKA KAIDIFIAKL FVKLKHIGLA 

       310        320        330        340        350        360 
NIFCDFAGKE ALNPEFLQDK VNVLNLYEAY NKYDYKAFFA KVDFLKEYLQ FGSAKNLAKI 


LNEI 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

AL111168 Genomic DNA. Translation: CAL34441.1.
PIRF81447.
RefSeqYP_002343729.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Genome annotation databases

GeneID904612.
GenomeReviewsGene locus Cj0288c in contig AL111168_GR.
KEGGcje:Cj0288c.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ9PIK8. FMPGSRK.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0288C-MON.
BRENDA2.4.1.182. 255835.

Family and domain databases

HAMAPMF_00392.
[Tree]
InterProIPR003835. Glyco_trans_19.
[Graphical view]
PfamPF02684. LpxB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00215. lpxB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPXB_CAMJE
AccessionPrimary (citable) accession number: Q9PIK8
Secondary accession number(s): Q0PBL8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents