Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5HWJ2 (LPXA_CAMJR)

Last modified November 3, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
      Short name=UDP-N-acetylglucosamine acyltransferase
    EC=2.3.1.129
Gene names
Name: lpxA
Ordered Locus Names: CJE0323
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity.

Catalytic activity

(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine. HAMAP MF_00387

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 1/6. HAMAP MF_00387

Subunit structure

Homotrimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid A biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP MF_00387
PRO_0000302566

Sequences

Sequence LengthMass (Da)Tools
Q5HWJ2-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 7235017BC7CBF2B7

FASTA26328,625
        10         20         30         40         50         60 
MKKIHPSAVI EEGAQLGDDV VVEAYAYVSK DAKIGNNVVI KQGARILSDT TIGDHSRVFS 

        70         80         90        100        110        120 
YAIVGDIPQD ISYKEEQKSG VVIGKNATIR EFATINSGTA KGDGFTRIGD NAFIMAYCHI 

       130        140        150        160        170        180 
AHDCLLGNNI ILANNATLAG HVELGDFTVV GGLTPIHQFV KVGEGCMIAG ASALSQDIVP 

       190        200        210        220        230        240 
FCLAEGNRAS IRSLNLVGTR RRFDKDEVDR LSRAFKTLFR QGDLKENAKN LLENQESENV 

       250        260 
KKMCHFILET KRGIPVYRGK NNA 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000025 Genomic DNA. Translation: AAW34913.1.
RefSeqYP_178343.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HWJ2.

Genome annotation databases

GeneID3231085.
GenomeReviewsGene locus CJE0323 in contig CP000025_GR.
KEGGcjr:CJE0323.
NMPDRfig|195099.3.peg.635.
TIGRCJE0323.

Phylogenomic databases

HOGENOMQ5HWJ2.
OMADLKYQGE.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_0323-MON.

Family and domain databases

HAMAPMF_00387.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_lpxA.
[Graphical view]
PfamPF00132. Hexapep. 7 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
TIGRFAMsTIGR01852. lipid_A_lpxA. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_CAMJR
AccessionPrimary (citable) accession number: Q5HWJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents