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Q9ZKY2 (LPXB_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:jhp_0801
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length360 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 – 360360Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000190170

Sequences

Sequence LengthMass (Da)Tools
Q9ZKY2 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 44A7504AC031BB2C

FASTA36041,566
        10         20         30         40         50         60 
MPTILVSALE ASSNIHLEEL RHNLPKDYRF IGVFESKEAL YSPREFSIMG FRDVIGRLGF 

        70         80         90        100        110        120 
LLKAHKEMVQ LAKQADMVLL MDSSSFNIPL AKKIKKQDPH KKIMYYILPQ VWAWKKWRAK 

       130        140        150        160        170        180 
SLEKYCDFLG AILPFEVGYY QKKAQYVGHP LLDEIKYYKK DIKGETLVFM PGSRKSEIAK 

       190        200        210        220        230        240 
MFPLFVKAAQ ILEQNEGFKR RVLVVPSFFK GLDLKALYGE DIKLFEISYD AHKSLFEAEF 

       250        260        270        280        290        300 
AFICSGTATL EAALIGTPFA LAYRAKTMDF LIARMLVNLH YIGLANIFYN ALNNETPGLG 

       310        320        330        340        350        360 
ESQLHPELIQ HFLSVEGLLK AYEEMDRERY FKESLRLREY LKHGSARKIA EEMAFLLNLT 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06363.1.
PIRD71888.
RefSeqNP_223519.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZKY2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp0801.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06363; AAD06363; jhp_0801.
GeneID890095.
KEGGhpj:jhp0801.
PATRIC20606337. VBIHelPyl98156_0873.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
KOK00748.
OMAIARMLVN.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-814-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZKY2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 76 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