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Q667K1 (LPXA_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:YPTB2991
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length262 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-Rule MF_00387

Catalytic activity

(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine. HAMAP-Rule 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-Rule MF_00387

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_00387

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00387.

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387
PRO_0000302617

Sequences

Sequence LengthMass (Da)Tools
Q667K1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C749FF7F53216DF8

FASTA26228,117
        10         20         30         40         50         60 
MIDKTAFIHP SSIVEEGAII GAGVYIGPFC IVGSQVEIGA GTELKSHVVV NGITKIGCDN 

        70         80         90        100        110        120 
QIYQFASIGE ANQDLKYAGE PTRVEVGDRN RIRESVTIHR GTTQGGGVTK VGCDNLLMVN 

       130        140        150        160        170        180 
THVAHDCVIG NRCILANNAA LGGHVEIDDY AIIGGMTAIH QFCVIGAHVM VGGCSGITQD 

       190        200        210        220        230        240 
VPPFVIAQGN HATPFGINIE GLKRRGFDKE SLHAIRSAYK LLYRSGRTLD EVKPEIAELA 

       250        260 
EQYPVVKAFN DFFARSTRGI IR 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH22229.1.
RefSeqYP_071497.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ667K1.
SMRQ667K1. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB2991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH22229; CAH22229; YPTB2991.
GeneID2955966.
KEGGyps:YPTB2991.
PATRIC18645165. VBIYerPse22266_3627.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1043.
HOGENOMHOG000294326.
KOK00677.
OMALEIGDRN.
OrthoDBEOG6F81P1.
ProtClustDBPRK05289.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-3092-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

HAMAPMF_00387. LpxA.
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 4 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01852. lipid_A_lpxA. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_YERPS
AccessionPrimary (citable) accession number: Q667K1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 65 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