Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5NEQ2 (LPXB_FRATT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:FTT_1568c
OrganismFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) [Reference proteome] [HAMAP]
Taxonomic identifier177416 [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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255182

Sequences

Sequence LengthMass (Da)Tools
Q5NEQ2 [UniParc].

Last modified February 1, 2005. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ749949 Genomic DNA. Translation: CAG46201.1.
RefSeqYP_170490.1. NC_006570.2.

3D structure databases

ProteinModelPortalQ5NEQ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177416.FTT_1568c.

Protocols and materials databases

DNASU3191793.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG46201; CAG46201; FTT_1568c.
GeneID3191793.
KEGGftu:FTT_1568c.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycFTUL177416:GNBP-1607-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_FRATT
AccessionPrimary (citable) accession number: Q5NEQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 57 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