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

Q8X8X8 (LPXA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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:Z0193, ECs0183
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_0000188048

Sequences

Sequence LengthMass (Da)Tools
Q8X8X8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: AE8A166F0045B45D

FASTA26228,050
        10         20         30         40         50         60 
MIDKSAFVHP TAIVEEGASI GANAHIGPFC IVGPHVEIGE GTVLKSHVVV NGHTKIGRDN 

        70         80         90        100        110        120 
EIYQFASIGE VNQDLKYAGE PTRVEIGDRN RIRESVTIHR GTVQGGGLTK VGSDNLLMIN 

       130        140        150        160        170        180 
AHIAHDCTVG NRCILANNAT LAGHVSVDDF AIIGGMAAVH QFCIIGAHVM VGGCSGVAQD 

       190        200        210        220        230        240 
VPPYVIAQGN HATPFGVNIE GLKRRGFSRE AITAIRNAYK LIYRSGKTLD EVKPEIAELA 

       250        260 
ETYPEVKAFT DFFARSTRGL IR 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54483.1.
BA000007 Genomic DNA. Translation: BAB33606.1.
PIRG85502.
G90651.
RefSeqNP_285875.1. NC_002655.2.
NP_308210.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X8X8.
SMRQ8X8X8. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54483; AAG54483; Z0193.
BAB33606; BAB33606; BAB33606.
GeneID913893.
956912.
KEGGece:Z0193.
ecs:ECs0183.
PATRIC18349312. VBIEscCol44059_0186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECOL386585:GJFA-181-MONOMER.
ECOO157:LPXA-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. 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_ECO57
AccessionPrimary (citable) accession number: Q8X8X8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 78 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