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Q02RB5 (LPXB_PSEAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:PA14_17220
OrganismPseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP]
Taxonomic identifier208963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length378 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 – 378378Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000049408

Sequences

Sequence LengthMass (Da)Tools
Q02RB5 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 46CEEEA4863C68B7

FASTA37841,280
        10         20         30         40         50         60 
MADGLRVALV AGEASGDILG SGLMQALRAR HPDIEFIGVG GPRMEAEGLS SYFPMERLSV 

        70         80         90        100        110        120 
MGLVEVLGRL PELLRRRKRL IRTLIEARPD VMIGIDAPDF TLGVEHKLRQ AGLRTVHYVS 

       130        140        150        160        170        180 
PSVWAWRQKR VLKIREACDL MLALFPFEAR FYEEHGVPVR FVGHPLANTI PLQADRAAAR 

       190        200        210        220        230        240 
ARLGLPADGQ VVALMPGSRG GEVGKLGALF LDTAQRLLVE RPGLRFVLPC ASAARREQIE 

       250        260        270        280        290        300 
QMLQGREPLP LTLLDGASHE ALAACDAVLI ASGTATLEAL LYKRPMVVAY RVAGLTYRIL 

       310        320        330        340        350        360 
KRLVKSPYIS LPNLLAGRLL VPELIQDAAT PQALAATLSP LLDDGSQQVE FFDAIHRALR 

       370 
QDASAQAAEA VLQLVERR 

« Hide

References

[1]"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial."
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.
Genome Biol. 7:R90.1-R90.14(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCBPP-PA14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ12876.1.
RefSeqYP_789521.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02RB5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208963.PA14_17220.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ12876; ABJ12876; PA14_17220.
GeneID4383256.
KEGGpau:PA14_17220.
PATRIC19848859. VBIPseAer79785_1401.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycPAER208963:GI5K-1385-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_PSEAB
AccessionPrimary (citable) accession number: Q02RB5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 47 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