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A4IWJ7 (LPXB_FRATW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:FTW_0358
OrganismFrancisella tularensis subsp. tularensis (strain WY96-3418) [Complete proteome] [HAMAP]
Taxonomic identifier418136 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length380 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 – 380380Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000049399

Sequences

Sequence LengthMass (Da)Tools
A4IWJ7 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 82D4B01962B0DF9C

FASTA38043,088
        10         20         30         40         50         60 
MRIGIVAGEL SGDQLGGTLV EALKQKYPNA IIEGIGGPKM AAAGFKSLYP MDALSLIGFL 

        70         80         90        100        110        120 
EIISKGLRIL SIRRKIINYF KQNKPDIFIG IDAPDFNLTV EKELRSAGIK TIHYVSPKIW 

       130        140        150        160        170        180 
VWREYRIKKI RKATDKILAI LPFETEYYKN RHKFEAIYVG HPLAKNIPIH IDRAKYRDKL 

       190        200        210        220        230        240 
GLKGSSLPIL SVLPGSRTTE VSRLLPLFLL ALQKLVDAGY KFKAIMPLAK PSLKPLFAKY 

       250        260        270        280        290        300 
KEQIDSLGIE VFETNSHDVL KASDLSLLAS GTATLEAMLC KLPMVVGYKL SWLSALIGRM 

       310        320        330        340        350        360 
LIGNHSYWAF PNILHKNEII KELIQEDCTV DNLFSELKRL FDDKRRNDYI VEEFEKIHKE 

       370        380 
MVIDTESKII QVLDTMIEKS 

« Hide

References

[1]"Complete genomic characterization of a pathogenic A.II strain of Francisella tularensis subspecies tularensis."
Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V., Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D., Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J., Wagner D.M., Brettin T.S. expand/collapse author list , Brown N., Gilna P., Keim P.S.
PLoS ONE 2:E947-E947(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WY96-3418.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000608 Genomic DNA. Translation: ABO46299.1.
RefSeqYP_001121419.1. NC_009257.1.

3D structure databases

ProteinModelPortalA4IWJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING418136.FTW_0358.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO46299; ABO46299; FTW_0358.
GeneID4959608.
KEGGftw:FTW_0358.
PATRIC17968038. VBIFraTul58433_0363.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycFTUL418136:GHXJ-331-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_FRATW
AccessionPrimary (citable) accession number: A4IWJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: May 14, 2014
This is version 44 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