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Q0BS63 (LPXB_GRABC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:GbCGDNIH1_1441
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter

Protein attributes

Sequence length393 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 – 393393Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000072224

Sequences

Sequence LengthMass (Da)Tools
Q0BS63 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: D2588B438EDED191

FASTA39342,932
        10         20         30         40         50         60 
MTAPLIYIVA GEHSGDVLGA RLIHALRAIN PSIRFAGIGG PRMEECGFQS LFPMHELAVM 

        70         80         90        100        110        120 
GLIEILPRVL KLRRRLQQTV QDIETRRPDL VLTIDSPGFC LRLLRAIQPF GIKRVHYVAP 

       130        140        150        160        170        180 
QVWAWREHRV KRFPGLWERM LCLLPFEEKW FAERNVPGQF VGHPVLESGA DQGDAARFRA 

       190        200        210        220        230        240 
RHSLADNARV IVLMPGSRAN EAGRLLPVYG ETLRLLMQNI PTITPVIPLA SSTAHTVRGA 

       250        260        270        280        290        300 
VSSWPVQPIF ITDIADKHDA FAAAEAALTK SGTSTLELAM GGVPMAVTYR VNRITAMMAR 

       310        320        330        340        350        360 
RLIRVPYVAM VNLLAGREIV PELLQENCTP TKIAAVLTSL MNNAPDTNGM GAADSQKQAL 

       370        380        390 
KAVVASLHAP NRHASDGLPS SAAAASIMEV LGQ 

« Hide

References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1260 / CGDNIH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000394 Genomic DNA. Translation: ABI62339.1.
RefSeqYP_745262.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BS63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391165.GbCGDNIH1_1441.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI62339; ABI62339; GbCGDNIH1_1441.
GeneID4274942.
KEGGgbe:GbCGDNIH1_1441.
PATRIC22079063. VBIGraBet83793_1493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycGBET391165:GHON-1478-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_GRABC
AccessionPrimary (citable) accession number: Q0BS63
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 50 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