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A1A7M6 (LPXB_ECOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Ecok1_01720
ORF Names:APECO1_1805
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length382 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 – 382382Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000049394

Sequences

Sequence LengthMass (Da)Tools
A1A7M6 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 2CFBE1A0F0620636

FASTA38242,355
        10         20         30         40         50         60 
MTEQRPLTIA LVAGETSGDI LGAGLIRALK ERVPNARFVG VAGPRMQAEG CEAWYEMEEL 

        70         80         90        100        110        120 
AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY 

       130        140        150        160        170        180 
VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNG 

       190        200        210        220        230        240 
ARDVLGIPYD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ 

       250        260        270        280        290        300 
FERIKAAVAP DLSVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF 

       310        320        330        340        350        360 
WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE 

       370        380 
LHQQIRCNAD EQAAQAVLEL AQ 

« Hide

References

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABI99665.1.
RefSeqYP_851380.1. NC_008563.1.

3D structure databases

ProteinModelPortalA1A7M6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405955.APECO1_1805.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI99665; ABI99665; APECO1_1805.
GeneID4494815.
KEGGecv:APECO1_1805.
PATRIC18211761. VBIEscCol127180_0194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_ECOK1
AccessionPrimary (citable) accession number: A1A7M6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: February 19, 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