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Q5HWH9 (LPXB_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipid-A-disaccharide synthase

EC=2.4.1.182
Gene names
Name:lpxB
Ordered Locus Names:CJE0336
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
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. HAMAP-Rule MF_00392

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-Rule MF_00392

Pathway

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

Sequence similarities

Belongs to the LpxB family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlipid-A-disaccharide synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255170

Sequences

Sequence LengthMass (Da)Tools
Q5HWH9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 54A93C17730DCC0D

FASTA36441,568
        10         20         30         40         50         60 
MKTFLVCALE PSANLHLKEV LKAYKKDFGE FELHGIYDES LCKEFDLNSK PLYSSHEFSA 

        70         80         90        100        110        120 
MGFIEVLPLI FKAKKAIKEL VNLTLSQTMD AVLCIDSPAF NIPFAKALKK AGSKIPRIYY 

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

       190        200        210        220        230        240 
FSKKDDEKTI AFLPGSRRSE IRRLMPIFKE LSQKFKGEKI 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]"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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW34926.1.
RefSeqYP_178356.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HWH9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE0336.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW34926; AAW34926; CJE0336.
GeneID3231098.
KEGGcjr:CJE0336.
PATRIC20042374. VBICamJej134361_0336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAAREIEYI.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-341-MONOMER.
UniPathwayUPA00359; UER00481.

Family and domain databases

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

Entry information

Entry nameLPXB_CAMJR
AccessionPrimary (citable) accession number: Q5HWH9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways