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P0A722

- LPXA_ECOLI

UniProt

P0A722 - LPXA_ECOLI

Protein

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

Gene

lpxA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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-KW

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10545. lpxA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki

    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.3 PublicationsUniRule annotation

    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 – 83
    Beta strandi12 – 143
    Beta strandi36 – 383
    Beta strandi52 – 565
    Beta strandi67 – 704
    Beta strandi83 – 864
    Beta strandi97 – 993
    Turni103 – 1064
    Beta strandi107 – 1115
    Beta strandi179 – 1813
    Beta strandi185 – 1884
    Turni189 – 1924
    Beta strandi193 – 1975
    Helixi199 – 2046
    Helixi209 – 22315
    Helixi229 – 24012
    Helixi244 – 2463
    Helixi247 – 2559

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00677.
    OMAiDCQDKKY.
    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

    MIDKSAFVHP TAIVEEGASI GANAHIGPFC IVGPHVEIGE GTVLKSHVVV    50
    NGHTKIGRDN EIYQFASIGE VNQDLKYAGE PTRVEIGDRN RIRESVTIHR 100
    GTVQGGGLTK VGSDNLLMIN AHIAHDCTVG NRCILANNAT LAGHVSVDDF 150
    AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD VPPYVIAQGN HATPFGVNIE 200
    GLKRRGFSRE AITAIRNAYK LIYRSGKTLD EVKPEIAELA ETYPEVKAFT 250
    DFFARSTRGL IR 262
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi E64742. XUECDP.
    RefSeqi NP_414723.1. NC_000913.3.
    YP_488483.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    4J09 X-ray 1.90 A 1-262 [» ]
    ProteinModelPortali P0A722.
    SMRi P0A722. Positions 1-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48043N.
    IntActi P0A722. 36 interactions.
    MINTi MINT-1234984.
    STRINGi 511145.b0181.

    Proteomic databases

    PaxDbi P0A722.
    PRIDEi P0A722.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73292 ; AAC73292 ; b0181 .
    BAA77856 ; BAA77856 ; BAA77856 .
    GeneIDi 12932097.
    944849.
    KEGGi ecj:Y75_p0177.
    eco:b0181.
    PATRICi 32115473. VBIEscCol129921_0188.

    Organism-specific databases

    EchoBASEi EB0540.
    EcoGenei EG10545. lpxA.

    Phylogenomic databases

    eggNOGi COG1043.
    HOGENOMi HOG000294326.
    KOi K00677.
    OMAi DCQDKKY.
    OrthoDBi EOG6F81P1.
    PhylomeDBi P0A722.

    Enzyme and pathway databases

    UniPathwayi UPA00359 ; UER00477 .
    BioCyci EcoCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.
    ECOL316407:JW0176-MONOMER.
    MetaCyc:UDPNACETYLGLUCOSAMACYLTRANS-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A722.
    PROi P0A722.

    Gene expression databases

    Genevestigatori P0A722.

    Family and domain databases

    Gene3Di 1.20.1180.10. 1 hit.
    HAMAPi MF_00387. LpxA.
    InterProi IPR029098. Acetyltransf_C.
    IPR001451. Hexapep_transf.
    IPR018357. Hexapep_transf_CS.
    IPR010137. Lipid_A_LpxA.
    IPR011004. Trimer_LpxA-like.
    [Graphical view ]
    Pfami PF13720. Acetyltransf_11. 1 hit.
    PF00132. Hexapep. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF000456. UDP-GlcNAc_acltr. 1 hit.
    SUPFAMi SSF51161. SSF51161. 1 hit.
    TIGRFAMsi TIGR01852. lipid_A_lpxA. 1 hit.
    PROSITEi PS00101. HEXAPEP_TRANSFERASES. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    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: October 1, 2014
    This is version 92 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