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Q2L147 (LPXB_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:BAV1747
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length395 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 – 395395Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255162

Sequences

Sequence LengthMass (Da)Tools
Q2L147 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: F33ADA25AC4537C4

FASTA39543,263
        10         20         30         40         50         60 
MSLSIGMVAG EPSGDLLAGR IIGGLRAGAP DVHCAGIGGP QMQAQGFEAW HPMHALTVFG 

        70         80         90        100        110        120 
YIDALKRIPS LLSIYGQTKQ RMLAERPAAF VGIDAPDFNL RLELQLRQAG IPTVHFVGPS 

       130        140        150        160        170        180 
IWAWRYERIH KIRAAVSHML VLFPFEEEIY QKEGIPVTYV GHPLAGVIPM RPDRAAARLR 

       190        200        210        220        230        240 
LNLDVGERVL AILPGSRSSE IRTLAPRFLQ AAQLLQARDP ALCCVVPMVN PQRRAEFEQI 

       250        260        270        280        290        300 
LAQYPVQGLR CITAEDVQGN GATPVAWSVM EAADAVLVAS GTATLETALY KRPMVISYVL 

       310        320        330        340        350        360 
TPWMRRIMAW KSGQQRPYLP WVGLPNVLLK DFAVPELLQD DATPEKLAEA AWTALTDKDN 

       370        380        390 
AARIEARFTA MHEELLRDTP ALAAKAILEV AHGAG 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ49355.1.
RefSeqYP_786265.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV1747.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6267311.
KEGGbav:BAV1747.
PATRIC21129680. VBIBorAvi43433_1761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAVI360910:GCKI-1774-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_BORA1
AccessionPrimary (citable) accession number: Q2L147
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 48 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