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A0Q7X9 (LPXB_FRATN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:FTN_1477
OrganismFrancisella tularensis subsp. novicida (strain U112) [Complete proteome] [HAMAP]
Taxonomic identifier401614 [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_1000049397

Sequences

Sequence LengthMass (Da)Tools
A0Q7X9 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: D1CF476843C10ED4

FASTA38043,117
        10         20         30         40         50         60 
MRIGIVAGEL SGDQLGGTLV EALKQKYPNA IIEGIGGPKM AAAGFKSLYP MDALSLIGFL 

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

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

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

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

       310        320        330        340        350        360 
LIGNHSYWAF PNILHKSEII KELIQEDCTV DNLFSELKRL FDDKQRNDYI VEEFEKIHKE 

       370        380 
MVIDTESKII QVLNTMIEKS 

« Hide

References

[1]"Comparison of Francisella tularensis genomes reveals evolutionary events associated with the emergence of human pathogenic strains."
Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y. expand/collapse author list , Chang J., Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.
Genome Biol. 8:R102.1-R102.16(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: U112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000439 Genomic DNA. Translation: ABK90344.1.
RefSeqYP_899098.1. NC_008601.1.

3D structure databases

ProteinModelPortalA0Q7X9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING401614.FTN_1477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK90344; ABK90344; FTN_1477.
GeneID4548572.
KEGGftn:FTN_1477.
PATRIC17936117. VBIFraNov128299_1509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBCLSK935090.

Enzyme and pathway databases

BioCycFNOV401614:GC4M-1476-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_FRATN
AccessionPrimary (citable) accession number: A0Q7X9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 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