Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B2UVD9 (LPXA_HELPS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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:HPSH_07115
OrganismHelicobacter pylori (strain Shi470) [Complete proteome] [HAMAP]
Taxonomic identifier512562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length270 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 – 270270Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387
PRO_1000122712

Sequences

Sequence LengthMass (Da)Tools
B2UVD9 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: C0E0865C1797E820

FASTA27029,939
        10         20         30         40         50         60 
MSKIAKTAII SPKAEIGKGV EIGEFCVIGD HIKLNDGVKL HNNVTLQGHT FIGKNTEIFP 

        70         80         90        100        110        120 
FAALGTQPQD LKYKGEYSEL IIGEDNLIRE FCMINPGTEG GIKKTIIGDK NLLMAYVHVA 

       130        140        150        160        170        180 
HDCVIGSHCI FANGVTLAGH IEIGDYVNIG GLTAIHQFVR IAKGCMIAGK SALGKDVPPY 

       190        200        210        220        230        240 
CTVEGNRAFI RGLNRHRMRQ LLESKDIDFI HVLYKRLFRP VPSLRESAKL ELEEHPNNPF 

       250        260        270 
VKEICSFILE SSRGVAYKSS EYSNEEKQEE 

« Hide

References

[1]"Genome sequence of Helicobacter pylori from the remote Amazon: traces of Asian ancestry of the first Americans."
Kersulyte D., Kalia A., Gilman R.H., Berg D.E.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Shi470.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001072 Genomic DNA. Translation: ACD48821.1.
RefSeqYP_001910851.1. NC_010698.2.

3D structure databases

ProteinModelPortalB2UVD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING512562.HPSH_07115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD48821; ACD48821; HPSH_07115.
GeneID6296809.
KEGGhps:HPSH_07115.
PATRIC20614183. VBIHelPyl23559_1380.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1043.
HOGENOMHOG000294326.
KOK00677.
OMADHIKLND.
OrthoDBEOG6F81P1.

Enzyme and pathway databases

BioCycHPYL512562:GHHZ-1420-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

Gene3D1.20.1180.10. 1 hit.
HAMAPMF_00387. LpxA.
InterProIPR029098. Acetyltransf_C.
IPR001451. Hexapep_transf.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 3 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01852. lipid_A_lpxA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPXA_HELPS
AccessionPrimary (citable) accession number: B2UVD9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: June 11, 2014
This is version 42 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