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Protein

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

Gene

lpxA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.

Catalytic activityi

(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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251Substrate
Binding sitei144 – 1441Substrate
Binding sitei161 – 1611Substrate

GO - Molecular functioni

  1. acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity Source: EcoliWiki
  2. identical protein binding Source: EcoCyc

GO - Biological processi

  1. lipid A biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
ECOL316407:JW0176-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
BRENDAi2.3.1.129. 2026.
UniPathwayiUPA00359; UER00477.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferaseUniRule annotation (EC:2.3.1.129UniRule annotation)
Short name:
UDP-N-acetylglucosamine acyltransferaseUniRule annotation
Gene namesi
Name:lpxAUniRule annotation
Ordered Locus Names:b0181, JW0176
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10545. lpxA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferasePRO_0000188046Add
BLAST

Proteomic databases

PaxDbiP0A722.
PRIDEiP0A722.

Expressioni

Gene expression databases

GenevestigatoriP0A722.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation3 Publications

Protein-protein interaction databases

DIPiDIP-48043N.
IntActiP0A722. 36 interactions.
MINTiMINT-1234984.
STRINGi511145.b0181.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Beta strandi12 – 143Combined sources
Beta strandi36 – 383Combined sources
Beta strandi52 – 565Combined sources
Beta strandi67 – 704Combined sources
Beta strandi83 – 864Combined sources
Beta strandi97 – 993Combined sources
Turni103 – 1064Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi185 – 1884Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1975Combined sources
Helixi199 – 2046Combined sources
Helixi209 – 22315Combined sources
Helixi229 – 24012Combined sources
Helixi244 – 2463Combined sources
Helixi247 – 2559Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4J09X-ray1.90A1-262[»]
ProteinModelPortaliP0A722.
SMRiP0A722. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A722.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 764Substrate binding

Sequence similaritiesi

Belongs to the transferase hexapeptide repeat family. LpxA subfamily.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1043.
HOGENOMiHOG000294326.
InParanoidiP0A722.
KOiK00677.
OMAiAPQDKKY.
OrthoDBiEOG6F81P1.
PhylomeDBiP0A722.

Family and domain databases

Gene3Di1.20.1180.10. 1 hit.
HAMAPiMF_00387. LpxA.
InterProiIPR029098. Acetyltransf_C.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 3 hits.
[Graphical view]
PIRSFiPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR01852. lipid_A_lpxA. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A722-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDKSAFVHP TAIVEEGASI GANAHIGPFC IVGPHVEIGE GTVLKSHVVV
60 70 80 90 100
NGHTKIGRDN EIYQFASIGE VNQDLKYAGE PTRVEIGDRN RIRESVTIHR
110 120 130 140 150
GTVQGGGLTK VGSDNLLMIN AHIAHDCTVG NRCILANNAT LAGHVSVDDF
160 170 180 190 200
AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD VPPYVIAQGN HATPFGVNIE
210 220 230 240 250
GLKRRGFSRE AITAIRNAYK LIYRSGKTLD EVKPEIAELA ETYPEVKAFT
260
DFFARSTRGL IR
Length:262
Mass (Da):28,080
Last modified:June 7, 2005 - v1
Checksum:iB42B076F0045B44C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 652QF → SV in AAC36918 (PubMed:3277952).Curated
Sequence conflicti125 – 1251H → D in AAC36918 (PubMed:3277952).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti189 – 1891G → S in strain: SM101; temperature-sensitive.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19334 Genomic DNA. Translation: AAC36918.1.
U70214 Genomic DNA. Translation: AAB08610.1.
U00096 Genomic DNA. Translation: AAC73292.1.
AP009048 Genomic DNA. Translation: BAA77856.2.
PIRiE64742. XUECDP.
RefSeqiNP_414723.1. NC_000913.3.
YP_488483.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73292; AAC73292; b0181.
BAA77856; BAA77856; BAA77856.
GeneIDi12932097.
944849.
KEGGiecj:Y75_p0177.
eco:b0181.
PATRICi32115473. VBIEscCol129921_0188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19334 Genomic DNA. Translation: AAC36918.1.
U70214 Genomic DNA. Translation: AAB08610.1.
U00096 Genomic DNA. Translation: AAC73292.1.
AP009048 Genomic DNA. Translation: BAA77856.2.
PIRiE64742. XUECDP.
RefSeqiNP_414723.1. NC_000913.3.
YP_488483.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4J09X-ray1.90A1-262[»]
ProteinModelPortaliP0A722.
SMRiP0A722. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48043N.
IntActiP0A722. 36 interactions.
MINTiMINT-1234984.
STRINGi511145.b0181.

Proteomic databases

PaxDbiP0A722.
PRIDEiP0A722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73292; AAC73292; b0181.
BAA77856; BAA77856; BAA77856.
GeneIDi12932097.
944849.
KEGGiecj:Y75_p0177.
eco:b0181.
PATRICi32115473. VBIEscCol129921_0188.

Organism-specific databases

EchoBASEiEB0540.
EcoGeneiEG10545. lpxA.

Phylogenomic databases

eggNOGiCOG1043.
HOGENOMiHOG000294326.
InParanoidiP0A722.
KOiK00677.
OMAiAPQDKKY.
OrthoDBiEOG6F81P1.
PhylomeDBiP0A722.

Enzyme and pathway databases

UniPathwayiUPA00359; UER00477.
BioCyciEcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
ECOL316407:JW0176-MONOMER.
MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
BRENDAi2.3.1.129. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A722.
PROiP0A722.

Gene expression databases

GenevestigatoriP0A722.

Family and domain databases

Gene3Di1.20.1180.10. 1 hit.
HAMAPiMF_00387. LpxA.
InterProiIPR029098. Acetyltransf_C.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 3 hits.
[Graphical view]
PIRSFiPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMiSSF51161. SSF51161. 1 hit.
TIGRFAMsiTIGR01852. lipid_A_lpxA. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1987) [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 (JAN-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 (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. 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(2005) [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(1986) [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(1994) [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(2005) [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(2006) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH UDP-3-O-(R-3-HYDROXYMYRISTOYL)-GLCNAC, SUBUNIT.

Entry informationi

Entry nameiLPXA_ECOLI
AccessioniPrimary (citable) accession number: P0A722
Secondary accession number(s): P10440, P78243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 1, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.