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A6SZN9 (LPXA_JANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:mma_2046
OrganismJanthinobacterium sp. (strain Marseille) (Minibacterium massiliensis) [Complete proteome] [HAMAP]
Taxonomic identifier375286 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeJanthinobacterium

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_1000013167

Sequences

Sequence LengthMass (Da)Tools
A6SZN9 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 4458599FB58BE500

FASTA26228,182
        10         20         30         40         50         60 
MSLIHPTAIV DPKAQLDSSV EVGPYTVIGP DVVIGAGSKI GPHVVVEGHT TIGADNKIFQ 

        70         80         90        100        110        120 
FASIGAAPQD KKYAGEPTLL TIGDRNTIRE FVTINLGTSQ DVGITRLGND NWIMAYVHIA 

       130        140        150        160        170        180 
HDCQLGSNII LANNATLAGH VHLEDWVFLG GFTSVHQFCR IGAHAMTAFT AAVSQDIPPF 

       190        200        210        220        230        240 
VTAAGNRAVP AGINSEGLKR RGFSSEQIMA IKRGYKTIYR SGLPLEEAKL ALQAEEEKSP 

       250        260 
DAAQYLRQLR EFIEASPRGI IR 

« Hide

References

[1]"Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria."
Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Marseille.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000269 Genomic DNA. Translation: ABR88824.1.
RefSeqYP_001353736.1. NC_009659.1.

3D structure databases

ProteinModelPortalA6SZN9.
SMRA6SZN9. Positions 2-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375286.mma_2046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR88824; ABR88824; mma_2046.
GeneID5352458.
KEGGmms:mma_2046.
PATRIC22156591. VBIJanSp106498_2065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycJSP375286:GJ8U-2083-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

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

Entry information

Entry nameLPXA_JANMA
AccessionPrimary (citable) accession number: A6SZN9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 46 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