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Q667K2 (LPXB_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:YPTB2990
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length394 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 – 394394Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255236

Sequences

Sequence LengthMass (Da)Tools
Q667K2 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: F4A481D7C188B25C

FASTA39443,261
        10         20         30         40         50         60 
MQNSPLTADC SLNAGRPLTI GLVAGETSGD ILGAGLIRAL KVQVPNARFV GVAGPLMQAE 

        70         80         90        100        110        120 
GCEAWYEMEE LAVMGVVEVL ERLPRLLKIR KDLTQRFSEL SPDVFVGIDA PDFNITLEGR 

       130        140        150        160        170        180 
LKQRGIRTIH YVSPSVWAWR QKRVFKIGKA TDMVLAFLPF EKAFYDRFNV PCRFIGHTMA 

       190        200        210        220        230        240 
DAMPLVPDQQ AARAELGIAP NATCLALLPG SRHSEVEMLS ADFLRTAVIL RDKLPNLEVV 

       250        260        270        280        290        300 
VPLVNSKRRE QFERIKAEIA PDLSVHLLDG KARVAMIASD AALLASGTAA LECMLAKCPM 

       310        320        330        340        350        360 
VVGYRMKPFT FWLAERLVKT PYVSLPNLLA GEELVTELLQ QECQPQKLAG ALLPLLQGGS 

       370        380        390 
EIAALKERFL VLHQSIRCGA DEQAAQAVLE LADR 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH22228.1.
RefSeqYP_071496.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ667K2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB2990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH22228; CAH22228; YPTB2990.
GeneID2955967.
KEGGyps:YPTB2990.
PATRIC18645163. VBIYerPse22266_3626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBPRK00025.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-3091-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_YERPS
AccessionPrimary (citable) accession number: Q667K2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 11, 2004
Last modified: February 19, 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

PATHWAY comments

Index of metabolic and biosynthesis pathways