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Q6G1J6 (LPXA_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:BQ06920
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length274 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 – 274274Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387
PRO_0000302563

Sequences

Sequence LengthMass (Da)Tools
Q6G1J6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 63C1B5F9D602539F

FASTA27429,453
        10         20         30         40         50         60 
MSGTKIHPTA LVEKGAQLGE NVFIGPFCHI GPEAVIDDGC SLMNHVVIMG KTTLGAKSKV 

        70         80         90        100        110        120 
FSHAVLGTDP QNNKHKGGYT TLSIGKNCTI REGVTMHRGS DSSVGMTIVG DDCQFFCYAH 

       130        140        150        160        170        180 
VAHDCRVGSH VTFANNAMIA GHVTVGDYVI IGGGSAVHQF VRIGHHAFIG GVSALVGDLI 

       190        200        210        220        230        240 
PYGTAVGVQA KLAGLNIIGM KRAGLERKDI HALRHAVAML FDHSKPFKER VNDVSSFYST 

       250        260        270 
SQSVLDVVNF IKEEGKRFYC TPKFEDDRIK VNKD 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26181.1.
RefSeqYP_032329.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6G1J6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ06920.

Proteomic databases

PRIDEQ6G1J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF26181; CAF26181; BQ06920.
GeneID2867062.
KEGGbqu:BQ06920.
PATRIC31952683. VBIBarQui58630_0767.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBQUI283165:GHZA-691-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. 3 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01852. lipid_A_lpxA. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_BARQU
AccessionPrimary (citable) accession number: Q6G1J6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 19, 2004
Last modified: February 19, 2014
This is version 66 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