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P0A722 (LPXA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:b0181, JW0176
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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. Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm HAMAP-Rule MF_00387.

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

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_0000188046

Regions

Region73 – 764Substrate binding HAMAP-Rule MF_00387

Sites

Binding site1251Substrate
Binding site1441Substrate
Binding site1611Substrate

Natural variations

Natural variant1891G → S in strain: SM101; temperature-sensitive.

Experimental info

Sequence conflict64 – 652QF → SV in AAC36918. Ref.1
Sequence conflict1251H → D in AAC36918. Ref.1

Secondary structure

................................. 262
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A722 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: B42B076F0045B44C

FASTA26228,080
        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 AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD 

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

       250        260 
ETYPEVKAFT DFFARSTRGL IR 

« Hide

References

« Hide 'large scale' references
[1]"First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene."
Coleman J., Raetz C.R.H.
J. Bacteriol. 170:1268-1274(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 64-65 AND 125.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase."
Crowell D.N., Reznikoff W.S., Raetz C.R.H.
J. Bacteriol. 169:5727-5734(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-262.
[7]"A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase."
Raetz C.R.H., Roderick S.L.
Science 270:997-1000(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
[8]"Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide."
Williams A.H., Immormino R.M., Gewirth D.T., Raetz C.R.
Proc. Natl. Acad. Sci. U.S.A. 103:10877-10882(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR, SUBUNIT.
[9]"Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis."
Ulaganathan V., Buetow L., Hunter W.N.
J. Mol. Biol. 369:305-312(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH UDP-N-ACETYL-GLUCOSAMINE, SUBUNIT.
[10]"Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase."
Williams A.H., Raetz C.R.
Proc. Natl. Acad. Sci. U.S.A. 104:13543-13550(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH UDP-3-O-(R-3-HYDROXYMYRISTOYL)-GLCNAC, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19334 Genomic DNA. Translation: AAC36918.1.
U70214 Genomic DNA. Translation: AAB08610.1.
U00096 Genomic DNA. Translation: AAC73292.1.
AP009048 Genomic DNA. Translation: BAA77856.2.
PIRXUECDP. E64742.
RefSeqNP_414723.1. NC_000913.3.
YP_488483.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXAX-ray2.60A1-262[»]
2AQ9X-ray1.80A1-262[»]
2JF2X-ray1.80A1-262[»]
2JF3X-ray3.00A1-262[»]
2QIAX-ray1.74A1-262[»]
2QIVX-ray1.85X1-262[»]
ProteinModelPortalP0A722.
SMRP0A722. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48043N.
IntActP0A722. 36 interactions.
MINTMINT-1234984.
STRING511145.b0181.

Proteomic databases

PaxDbP0A722.
PRIDEP0A722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73292; AAC73292; b0181.
BAA77856; BAA77856; BAA77856.
GeneID12932097.
944849.
KEGGecj:Y75_p0177.
eco:b0181.
PATRIC32115473. VBIEscCol129921_0188.

Organism-specific databases

EchoBASEEB0540.
EcoGeneEG10545. lpxA.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycEcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
ECOL316407:JW0176-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
UniPathwayUPA00359; UER00477.

Gene expression databases

GenevestigatorP0A722.

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...

Other

EvolutionaryTraceP0A722.
PROP0A722.

Entry information

Entry nameLPXA_ECOLI
AccessionPrimary (citable) accession number: P0A722
Secondary accession number(s): P10440, P78243
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 19, 2014
This is version 88 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene