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B7V7U5 (LPXB_PSEA8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:PLES_13921
OrganismPseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]
Taxonomic identifier557722 [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_1000123055

Sequences

Sequence LengthMass (Da)Tools
B7V7U5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 46DB015E89C9874D

FASTA37841,294
        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 VLALMPGSRG 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]"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LESB58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM209186 Genomic DNA. Translation: CAW26120.1.
RefSeqYP_002438996.1. NC_011770.1.

3D structure databases

ProteinModelPortalB7V7U5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557722.PLES_13921.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW26120; CAW26120; PLES_13921.
GeneID7180255.
KEGGpag:PLES_13921.
PATRIC19812360. VBIPseAer113719_1439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBPRK00025.

Enzyme and pathway databases

BioCycPAER557722:GHJW-1409-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_PSEA8
AccessionPrimary (citable) accession number: B7V7U5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 35 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