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B2JZ22 (LPXA_YERPB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:YPTS_3111
OrganismYersinia pseudotuberculosis serotype IB (strain PB1/+) [Complete proteome] [HAMAP]
Taxonomic identifier502801 [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_1000190870

Sequences

Sequence LengthMass (Da)Tools
B2JZ22 [UniParc].

Last modified June 10, 2008. 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]"Complete sequence of Yersinia pseudotuberculosis PB1/+."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PB1/+.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001048 Genomic DNA. Translation: ACC90066.1.
RefSeqYP_001873523.1. NC_010634.1.

3D structure databases

ProteinModelPortalB2JZ22.
SMRB2JZ22. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING502801.YPTS_3111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC90066; ACC90066; YPTS_3111.
GeneID6258282.
KEGGypb:YPTS_3111.
PATRIC18654389. VBIYerPse20639_3387.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1043.
HOGENOMHOG000294326.
KOK00677.
OMADCQDKKY.
OrthoDBEOG6F81P1.

Enzyme and pathway databases

BioCycYPSE502801:GHIH-3246-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. 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_YERPB
AccessionPrimary (citable) accession number: B2JZ22
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: June 11, 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