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B7V7U4 (LPXA_PSEA8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:PLES_13911
OrganismPseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]
Taxonomic identifier557722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length258 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 – 258258Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387
PRO_1000122720

Sequences

Sequence LengthMass (Da)Tools
B7V7U4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: B40E9923058E259E

FASTA25828,010
        10         20         30         40         50         60 
MSLIDPRAII DPSARLAADV QVGPWSIVGA EVEIGEGTVI GPHVVLKGPT KIGKHNRIYQ 

        70         80         90        100        110        120 
FSSVGEDTPD LKYKGEPTRL VIGDHNVIRE GVTIHRGTVQ DRAETTIGDH NLIMAYAHIG 

       130        140        150        160        170        180 
HDSVIGNHCI LVNNTALAGH VHVDDWAILS GYTLVHQYCR IGAHSFSGMG SAIGKDVPAY 

       190        200        210        220        230        240 
VTVFGNPAEA RSMNFEGMRR RGFSSEAIHA LRRAYKVVYR QGHTVEEALA ELAESAAQFP 

       250 
EVAVFRDSIQ SATRGITR 

« Hide

References

[1]"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LESB58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM209186 Genomic DNA. Translation: CAW26119.1.
RefSeqYP_002438995.1. NC_011770.1.

3D structure databases

ProteinModelPortalB7V7U4.
SMRB7V7U4. Positions 2-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557722.PLES_13911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW26119; CAW26119; PLES_13911.
GeneID7179903.
KEGGpag:PLES_13911.
PATRIC19812358. VBIPseAer113719_1438.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPAER557722:GHJW-1408-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

HAMAPMF_00387. LpxA.
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
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.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXA_PSEA8
AccessionPrimary (citable) accession number: B7V7U4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 39 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