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Q9X6P4 (LPXA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. 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:
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:PA3644
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length258 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
Reference proteome
Gene Ontology (GO)
   Biological processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP MF_00387
PRO_0000188058

Sequences

Sequence LengthMass (Da)Tools
Q9X6P4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B40E9923058E259E

FASTA25828,010
        10         20         30         40         50         60 
MSLIDPRAII DPSARLAADV QVGPWSIVGA EVEIGEGTVI GPHVVLKGPT KIGKHNRIYQ 

        70         80         90        100        110        120 
FSSVGEDTPD LKYKGEPTRL VIGDHNVIRE GVTIHRGTVQ DRAETTIGDH NLIMAYAHIG 

       130        140        150        160        170        180 
HDSVIGNHCI LVNNTALAGH VHVDDWAILS GYTLVHQYCR IGAHSFSGMG SAIGKDVPAY 

       190        200        210        220        230        240 
VTVFGNPAEA RSMNFEGMRR RGFSSEAIHA LRRAYKVVYR QGHTVEEALA ELAESAAQFP 

       250 
EVAVFRDSIQ SATRGITR 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning of a Pseudomonas gene encoding a hydroxydecanoyl-acyl carrier protein-dependent UDP-GlcNAc acyltransferase."
Dotson G.D., Kaltashov I.A., Cotter R.J., Raetz C.R.H.
J. Bacteriol. 180:330-337(1998) [PubMed: 9440522] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF142597 Genomic DNA. Translation: AAD30149.1.
AE004091 Genomic DNA. Translation: AAG07032.1.
PIRD83190.
RefSeqNP_252334.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9X6P4.
SMRQ9X6P4. Positions 2-258.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880493.
GenomeReviewsGene locus PA3644 in contig AE004091_GR.
KEGGpae:PA3644.
PATRIC19841911. VBIPseAer58763_3813.

Organism-specific databases

PseudoCAPPA3644.

Phylogenomic databases

HOGENOMHBG659295.
OMAREFCTFN.
ProtClustDBPRK05289.

Enzyme and pathway databases

BioCycPAER208964:PA3644-MONOMER.

Family and domain databases

HAMAPMF_00387. LpxA.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_lpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK00677.
PfamPF00132. Hexapep. 3 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01852. Lipid_A_lpxA. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_PSEAE
AccessionPrimary (citable) accession number: Q9X6P4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families