Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q9PIM1 (LPXA_CAMJE)

Last modified February 9, 2010. Version 59. 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: Cj0274
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
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. HAMAP MF_00387

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. HAMAP MF_00387

Subcellular location

Cytoplasm By similarity HAMAP MF_00387.

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_0000188038

Sequences

Sequence LengthMass (Da)Tools
Q9PIM1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C3D17D1BE12F9F01

FASTA26328,651
        10         20         30         40         50         60 
MKKIHPSAVI EEGAQLGDDV VIEAYAYVSK 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 IRSLNLVGIR RRFDKDEVDR LSRAFKTLFR QGDLKENAKN LLENQESENV 

       250        260 
KKMCHFILET KRGIPVYRGK NNA 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34428.1.
PIRA81446.
RefSeqYP_002343716.1.

3D structure databases

SMRQ9PIM1. Positions 2-256.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PIM1. 31 interactions.

Genome annotation databases

GeneID904599.
GenomeReviewsGene locus Cj0274 in contig AL111168_GR.
KEGGcje:Cj0274.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG659295.
OMADLKYQGE.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0274-MONOMER.
BRENDA2.3.1.129. 255835.

Family and domain databases

HAMAPMF_00387. LpxA.
[Tree]
InterProIPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_lpxA.
IPR011004. Trimer_LpxA-like.
[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_CAMJE
AccessionPrimary (citable) accession number: Q9PIM1
Secondary accession number(s): Q0PBN1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 59 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