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Q92II0 (LPXB_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RC0440
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length446 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.

Contains 1 RPE3 insert domain.

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 – 446446Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000190181

Regions

Domain379 – 41840RPE3 insert

Sequences

Sequence LengthMass (Da)Tools
Q92II0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: FD5F11728238FDB7

FASTA44650,738
        10         20         30         40         50         60 
MIKIYFIAGE VSGDFVGGRI MQHLKNNTGV QLNSPVSSFV NDAVQFVGVG GKYMEEAGSF 

        70         80         90        100        110        120 
KSLFPITSIN LMGFVEILPH IFKLKKLIDK TVEDIINSKA DLLITIDSPG FTYRVAKRVR 

       130        140        150        160        170        180 
KLLPKLKMIH IVAPSVWAYK EGRAVKYAKI YDCLFALLPF EPPYFTKVGL DCRYIGHPIM 

       190        200        210        220        230        240 
EQEFYSDKIA LREEFKIDEN ERVLCVTLGS RKGEILRHLS VFVSSIEEIF KSCNNLKVIF 

       250        260        270        280        290        300 
TLANPAHEAI IKPFLEDVKF NYLFSSERLK IYAVADVALA KSGTNTLEIA ASGTPMIVAY 

       310        320        330        340        350        360 
KVNLISFFII RLLIKIKYVT LINIIADKEI IPEFIQFNCR ANLISNKLQE LLFNSKKAYE 

       370        380        390        400        410        420 
QVIESQKILQ QLGFKSNRLQ LNSESFRHDE FKGKLARCTK VREHRLSLEN SLVSSDRDDA 

       430        440 
VPSYIAAAII KQEFLEPKIK LLKEKD 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02978.1.
PIRH97754.
RefSeqNP_360077.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92II0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0440.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Proteomic databases

PRIDEQ92II0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02978; AAL02978; RC0440.
GeneID928676.
KEGGrco:RC0440.
PATRIC17888085. VBIRicCon45613_0498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

UniPathwayUPA00359; UER00481.

Family and domain databases

HAMAPMF_00392. LpxB.
InterProIPR003835. Glyco_trans_19.
IPR022437. RPE3.
[Graphical view]
PfamPF02684. LpxB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00215. lpxB. 1 hit.
TIGR03775. RPE3. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPXB_RICCN
AccessionPrimary (citable) accession number: Q92II0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 66 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

Rickettsia conorii

(strain Malish 7): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways