Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase

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P0A722 (LPXA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid A biosynthesis Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from direct assay PubMed 3549716. Source: EcoliWiki
Molecular_function	acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity Inferred from direct assay PubMed 3549716. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 262

262

Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387

PRO_0000188046

Regions

Region

73 – 76

Substrate binding HAMAP-Rule MF_00387

Sites

Binding site

125

Substrate

Binding site

144

Substrate

Binding site

161

Substrate

Natural variations

Natural variant

189

G → S in strain: SM101; temperature-sensitive.

Experimental info

Sequence conflict

64 – 65

QF → SV in AAC36918. Ref.1

Sequence conflict

125

H → D in AAC36918. Ref.1

Secondary structure

262

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A722 [UniParc].

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

262

28,080

        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' referencesShow '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 277:1453-1474(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.

PIR

XUECDP. E64742.

RefSeq

NP_414723.1. NC_000913.2.
YP_488483.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LXA	X-ray	2.60	A	1-262	[»]
2AQ9	X-ray	1.80	A	1-262	[»]
2JF2	X-ray	1.80	A	1-262	[»]
2JF3	X-ray	3.00	A	1-262	[»]
2QIA	X-ray	1.74	A	1-262	[»]
2QIV	X-ray	1.85	X	1-262	[»]

ProteinModelPortal

P0A722.

SMR

P0A722. Positions 1-262.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48043N.

IntAct

P0A722. 36 interactions.

MINT

MINT-1234984.

STRING

511145.b0181.

Proteomic databases

PaxDb

P0A722.

PRIDE

P0A722.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73292; AAC73292; b0181.
BAA77856; BAA77856; BAA77856.

GeneID

12932097.
944849.

KEGG

ecj:Y75_p0177.
eco:b0181.

PATRIC

32115473. VBIEscCol129921_0188.

Organism-specific databases

EchoBASE

EB0540.

EcoGene

EG10545. lpxA.

Phylogenomic databases

eggNOG

COG1043.

HOGENOM

HOG000294326.

K00677.

OMA

REFCTFN.

ProtClustDB

PRK05289.

Enzyme and pathway databases

BioCyc

EcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
ECOL316407:JW0176-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.

UniPathway

UPA00359; UER00477.

Gene expression databases

Genevestigator

P0A722.

Family and domain databases

HAMAP

MF_00387. LpxA.

InterPro

IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]

Pfam

PF00132. Hexapep. 5 hits.
[Graphical view]

PIRSF

PIRSF000456. UDP-GlcNAc_acltr. 1 hit.

SUPFAM

SSF51161. Trimer_LpxA_like. 1 hit.

TIGRFAMs

TIGR01852. lipid_A_lpxA. 1 hit.

PROSITE

PS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A722.

Entry information

Entry name

LPXA_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents