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

Q68X51 (LPXB_RICTY) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RT0311
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

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_0000255219

Sequences

Sequence LengthMass (Da)Tools
Q68X51 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E55063452071B13F

FASTA38043,320
        10         20         30         40         50         60 
MKKIYFIAGE MSGDFIGGHI IQNLKSNEGL EFTGIGGQYM EEAGNFKSLF TITAINFIGF 

        70         80         90        100        110        120 
IEIIPHLLKI KKLIDKTVEN IINSKVDLLI TIDSPGFTYR VAKRVRKFLP NLKIIHIVAP 

       130        140        150        160        170        180 
SVWAYKAGRA VDYAKIYDCL FALLPFEPPY FTKVGLDCRY IGHPILEQEF YRDKIALRKE 

       190        200        210        220        230        240 
FKIDDNESIL CVTFGTRKGE ILRHLPIFIT AIQKISKDYK NLRIIFPLVH PDHEAIIKPF 

       250        260        270        280        290        300 
LENVQFNYLF LSSERLKAYA VSDLALAKSG TNTLEISASG TPMVVAYKVN IISFFIIMFL 

       310        320        330        340        350        360 
IKIKYVSLIN IMAGSAIIPE FIQFNCRANL ISNKLKELLS NSQKRDNQVV ESQKILQKLR 

       370        380 
FASDRSPSYI AAKIIKQEFL 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU03791.1.
RefSeqYP_067273.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68X51.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU03791; AAU03791; RT0311.
GeneID2958828.
KEGGrty:RT0311.
PATRIC17909814. VBIRicTyp34752_0322.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAIARMLVN.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-326-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_RICTY
AccessionPrimary (citable) accession number: Q68X51
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 11, 2004
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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways