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Q17ZK1 (LPXA_HELAH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 59. 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:Hac_0063
OrganismHelicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]
Taxonomic identifier382638 [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_0000302578

Sequences

Sequence LengthMass (Da)Tools
Q17ZK1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: DCB781EA4C8FEB99

FASTA27029,622
        10         20         30         40         50         60 
MSKIAKTAII SPKAEVGKGV EIGEFCVIGD GIKLDDGVKL HNNVTLQGHT FIGKNTEIFP 

        70         80         90        100        110        120 
FVVLGTQPQD LKYKGEYSEL IVGEDNLIRE FCMINPGTEG GIKKTIIGDK NLLMAYVHVA 

       130        140        150        160        170        180 
HDCVIGNHCI LANGVTLAGH VEVGDYVNIG GLTAIHQFVR IAKGSMIAGK SALGKDVPPY 

       190        200        210        220        230        240 
CLAEGNRAFI KGLNRHRMRQ LLESKDIDFI HALYKRLFRP VLSLRESAKL ELEEHANNPI 

       250        260        270 
VEEICSFILA SSRGVAYKSS EYSSEEKQED 

« Hide

References

[1]"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sheeba.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260522 Genomic DNA. Translation: CAJ98925.1.
RefSeqYP_663924.1. NC_008229.1.

3D structure databases

ProteinModelPortalQ17ZK1.
SMRQ17ZK1. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382638.Hac_0063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ98925; CAJ98925; Hac_0063.
GeneID4177620.
KEGGhac:Hac_0063.
PATRIC20584064. VBIHelAci71660_0065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1043.
HOGENOMHOG000294326.
KOK00677.
OMADHIKLND.
OrthoDBEOG6F81P1.

Enzyme and pathway databases

BioCycHACI382638:GJAU-59-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

Gene3D1.20.1180.10. 1 hit.
HAMAPMF_00387. LpxA.
InterProIPR029098. Acetyltransf_C.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
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.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_HELAH
AccessionPrimary (citable) accession number: Q17ZK1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 25, 2006
Last modified: June 11, 2014
This is version 59 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