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Protein

UDP-3-O-acyl-N-acetylglucosamine deacetylase

Gene

lpxC

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

Functioni

Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.UniRule annotation4 Publications

Catalytic activityi

UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H2O = UDP-3-O-((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate.UniRule annotation5 Publications

Cofactori

Zn2+UniRule annotation2 Publications, Fe2+2 PublicationsNote: Can use either Fe2+ or Zn2+. The metal cofactor can switch between Fe2+ and Zn2+ in response to metal availability. Metal switching may be important for regulating the LpxC activity upon changes in environmental conditions. Has a significantly higher affinity for Zn2+, but exhibits higher activity with Fe2+ (PubMed:20136146, PubMed:20709752). Can also use Co2+, Ni2+ and, to a lesser extent, Mn2+ (PubMed:10026271).3 Publications

Enzyme regulationi

Regulation occurs at the protein level, via degradation of LpxC by the FtsH protease (PubMed:10048027, PubMed:16420369, PubMed:21193611, PubMed:23417489). Degradation is growth rate-dependent. LpxC is degraded rapidly during slow growth, probably to avoid toxic overproduction of lipopolysaccharides, but is highly stable under optimal growth conditions (PubMed:23417489). Increased amounts of LpxC are made under conditions that reduce the lipid A content of cells (PubMed:8824222). Inhibited by metal chelators such as EDTA and dipicolinic acid (DPA) and by high concentrations of Zn2+ (PubMed:10026271).6 Publications

Kineticsi

kcat is 3.3 sec(-1) at 30 degrees Celsius. kcat is 0.09 sec(-1) at 1 degree Celsius.1 Publication

  1. KM=2.1 µM for UDP-3-O-myristoyl-N-acetylglucosamine (at 30 degrees Celsius)1 Publication
  2. KM=0.6 µM for UDP-3-O-myristoyl-N-acetylglucosamine (at 1 degree Celsius)1 Publication

    Pathwayi: lipid IV(A) biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation1 Publication
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
    2. UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
    3. UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD)
    4. UDP-2,3-diacylglucosamine hydrolase (lpxH)
    5. Lipid-A-disaccharide synthase (lpxB)
    6. Tetraacyldisaccharide 4'-kinase (lpxK)
    This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi79 – 791Zinc; via tele nitrogenUniRule annotation2 Publications
    Metal bindingi238 – 2381Zinc; via tele nitrogenUniRule annotation2 Publications
    Metal bindingi242 – 2421ZincUniRule annotation2 Publications
    Active sitei265 – 2651Proton donorUniRule annotation2 Publications

    GO - Molecular functioni

    • deacetylase activity Source: EcoliWiki
    • iron ion binding Source: EcoCyc
    • UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity Source: EcoCyc
    • zinc ion binding Source: EcoCyc

    GO - Biological processi

    • lipid A biosynthetic process Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:UDPACYLGLCNACDEACETYL-MONOMER.
    ECOL316407:JW0094-MONOMER.
    MetaCyc:UDPACYLGLCNACDEACETYL-MONOMER.
    UniPathwayiUPA00359; UER00478.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-3-O-acyl-N-acetylglucosamine deacetylase1 PublicationUniRule annotation (EC:3.5.1.108UniRule annotation5 Publications)
    Short name:
    UDP-3-O-acyl-GlcNAc deacetylase2 PublicationsUniRule annotation
    Alternative name(s):
    Protein EnvACurated
    UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase1 PublicationUniRule annotation
    Gene namesi
    Name:lpxC1 PublicationUniRule annotation
    Synonyms:asmB1 Publication, envA1 Publication
    Ordered Locus Names:b0096, JW0094
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10265. lpxC.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191H → A: 1400-fold decrease in activity. 1 Publication
    Mutagenesisi19 – 191H → Q: 90-fold decrease in activity. 1 Publication
    Mutagenesisi19 – 191H → Y: 200-fold decrease in activity. 1 Publication
    Mutagenesisi63 – 631C → A: Reduces level of inhibition by metal ions. 1 Publication
    Mutagenesisi78 – 781E → A: 700-fold decrease in activity. 1 Publication
    Mutagenesisi78 – 781E → Q: 3000-fold decrease in activity. 1 Publication
    Mutagenesisi79 – 791H → A: 2300-fold decrease in activity. 1 Publication
    Mutagenesisi79 – 791H → Q: 1200-fold decrease in activity. 1 Publication
    Mutagenesisi238 – 2381H → A: 1100-fold decrease in activity. 1 Publication
    Mutagenesisi242 – 2421D → A: 10-fold decrease in activity. 1 Publication
    Mutagenesisi242 – 2421D → Q: 2300-fold decrease in activity. 1 Publication
    Mutagenesisi246 – 2461D → A: 1800-fold decrease in activity. 1 Publication
    Mutagenesisi265 – 2651H → A: 3800-fold decrease in activity. 1 Publication
    Mutagenesisi265 – 2651H → Q: 5600-fold decrease in activity. 1 Publication

    Chemistry

    ChEMBLiCHEMBL5244.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305UDP-3-O-acyl-N-acetylglucosamine deacetylasePRO_0000191929Add
    BLAST

    Post-translational modificationi

    Degraded by FtsH.4 Publications

    Proteomic databases

    PaxDbiP0A725.

    Interactioni

    Protein-protein interaction databases

    BioGridi4261858. 357 interactions.
    DIPiDIP-48045N.
    IntActiP0A725. 5 interactions.
    MINTiMINT-1309717.
    STRINGi511145.b0096.

    Chemistry

    BindingDBiP0A725.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97Combined sources
    Beta strandi11 – 166Combined sources
    Turni18 – 203Combined sources
    Beta strandi22 – 298Combined sources
    Beta strandi37 – 415Combined sources
    Beta strandi43 – 464Combined sources
    Beta strandi48 – 514Combined sources
    Helixi54 – 563Combined sources
    Beta strandi61 – 633Combined sources
    Beta strandi65 – 673Combined sources
    Beta strandi73 – 753Combined sources
    Helixi78 – 8710Combined sources
    Beta strandi91 – 10010Combined sources
    Beta strandi106 – 1083Combined sources
    Helixi109 – 11810Combined sources
    Beta strandi120 – 1267Combined sources
    Beta strandi129 – 1324Combined sources
    Beta strandi136 – 1405Combined sources
    Beta strandi143 – 1486Combined sources
    Beta strandi151 – 1588Combined sources
    Helixi168 – 1703Combined sources
    Beta strandi171 – 1766Combined sources
    Helixi179 – 1857Combined sources
    Turni186 – 1883Combined sources
    Beta strandi192 – 1943Combined sources
    Helixi195 – 2028Combined sources
    Turni203 – 2053Combined sources
    Beta strandi214 – 2185Combined sources
    Beta strandi220 – 2234Combined sources
    Helixi234 – 24714Combined sources
    Helixi248 – 2503Combined sources
    Beta strandi254 – 2629Combined sources
    Helixi265 – 27713Combined sources
    Helixi279 – 2813Combined sources
    Beta strandi282 – 2854Combined sources
    Helixi290 – 2923Combined sources
    Helixi295 – 2973Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IS9X-ray2.13A/B1-300[»]
    4ISAX-ray1.80A1-300[»]
    4MDTX-ray2.59A/B/C/D1-305[»]
    4MQYX-ray2.00A1-305[»]
    ProteinModelPortaliP0A725.
    SMRiP0A725. Positions 1-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminus is required for deacetylase activity. The C-terminus contains a signal sequence necessary for FtsH-dependent degradation.1 Publication

    Sequence similaritiesi

    Belongs to the LpxC family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C7C. Bacteria.
    COG0774. LUCA.
    HOGENOMiHOG000256663.
    InParanoidiP0A725.
    KOiK02535.
    OMAiNSMLVKA.
    OrthoDBiEOG6PGK74.
    PhylomeDBiP0A725.

    Family and domain databases

    Gene3Di3.30.1700.10. 1 hit.
    3.30.230.20. 1 hit.
    HAMAPiMF_00388. LpxC.
    InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
    IPR004463. UDP-acyl_GlcNac_deAcase.
    IPR011334. UDP-acyl_GlcNac_deAcase_C.
    IPR015870. UDP-acyl_N-AcGlcN_deAcase_N.
    [Graphical view]
    PfamiPF03331. LpxC. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    TIGRFAMsiTIGR00325. lpxC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A725-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIKQRTLKRI VQATGVGLHT GKKVTLTLRP APANTGVIYR RTDLNPPVDF
    60 70 80 90 100
    PADAKSVRDT MLCTCLVNEH DVRISTVEHL NAALAGLGID NIVIEVNAPE
    110 120 130 140 150
    IPIMDGSAAP FVYLLLDAGI DELNCAKKFV RIKETVRVED GDKWAEFKPY
    160 170 180 190 200
    NGFSLDFTID FNHPAIDSSN QRYAMNFSAD AFMRQISRAR TFGFMRDIEY
    210 220 230 240 250
    LQSRGLCLGG SFDCAIVVDD YRVLNEDGLR FEDEFVRHKM LDAIGDLFMC
    260 270 280 290 300
    GHNIIGAFTA YKSGHALNNK LLQAVLAKQE AWEYVTFQDD AELPLAFKAP

    SAVLA
    Length:305
    Mass (Da):33,956
    Last modified:June 7, 2005 - v1
    Checksum:iCA439A00813463AB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501F → S in ASMB2/3; reduced activity. 1 Publication
    Natural varianti210 – 2101G → S in ASMB1; reduced activity. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M19211 Genomic DNA. Translation: AAA83849.1.
    X55034 Genomic DNA. Translation: CAA38873.1.
    U00096 Genomic DNA. Translation: AAC73207.1.
    AP009048 Genomic DNA. Translation: BAB96664.1.
    PIRiA28381. BVECEA.
    RefSeqiNP_414638.1. NC_000913.3.
    WP_000595482.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73207; AAC73207; b0096.
    BAB96664; BAB96664; BAB96664.
    GeneIDi944816.
    KEGGiecj:JW0094.
    eco:b0096.
    PATRICi32115297. VBIEscCol129921_0100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M19211 Genomic DNA. Translation: AAA83849.1.
    X55034 Genomic DNA. Translation: CAA38873.1.
    U00096 Genomic DNA. Translation: AAC73207.1.
    AP009048 Genomic DNA. Translation: BAB96664.1.
    PIRiA28381. BVECEA.
    RefSeqiNP_414638.1. NC_000913.3.
    WP_000595482.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IS9X-ray2.13A/B1-300[»]
    4ISAX-ray1.80A1-300[»]
    4MDTX-ray2.59A/B/C/D1-305[»]
    4MQYX-ray2.00A1-305[»]
    ProteinModelPortaliP0A725.
    SMRiP0A725. Positions 1-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261858. 357 interactions.
    DIPiDIP-48045N.
    IntActiP0A725. 5 interactions.
    MINTiMINT-1309717.
    STRINGi511145.b0096.

    Chemistry

    BindingDBiP0A725.
    ChEMBLiCHEMBL5244.

    Proteomic databases

    PaxDbiP0A725.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73207; AAC73207; b0096.
    BAB96664; BAB96664; BAB96664.
    GeneIDi944816.
    KEGGiecj:JW0094.
    eco:b0096.
    PATRICi32115297. VBIEscCol129921_0100.

    Organism-specific databases

    EchoBASEiEB0261.
    EcoGeneiEG10265. lpxC.

    Phylogenomic databases

    eggNOGiENOG4105C7C. Bacteria.
    COG0774. LUCA.
    HOGENOMiHOG000256663.
    InParanoidiP0A725.
    KOiK02535.
    OMAiNSMLVKA.
    OrthoDBiEOG6PGK74.
    PhylomeDBiP0A725.

    Enzyme and pathway databases

    UniPathwayiUPA00359; UER00478.
    BioCyciEcoCyc:UDPACYLGLCNACDEACETYL-MONOMER.
    ECOL316407:JW0094-MONOMER.
    MetaCyc:UDPACYLGLCNACDEACETYL-MONOMER.

    Miscellaneous databases

    PROiP0A725.

    Family and domain databases

    Gene3Di3.30.1700.10. 1 hit.
    3.30.230.20. 1 hit.
    HAMAPiMF_00388. LpxC.
    InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
    IPR004463. UDP-acyl_GlcNac_deAcase.
    IPR011334. UDP-acyl_GlcNac_deAcase_C.
    IPR015870. UDP-acyl_N-AcGlcN_deAcase_N.
    [Graphical view]
    PfamiPF03331. LpxC. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    TIGRFAMsiTIGR00325. lpxC. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli."
      Beall B., Lutkenhaus J.
      J. Bacteriol. 169:5408-5415(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli."
      Yi Q.-M., Lutkenhaus J.
      Gene 36:241-247(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
      Strain: K12.
    6. "The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase."
      Young K., Silver L.L., Bramhill D., Cameron P., Eveland S.S., Raetz C.R., Hyland S.A., Anderson M.S.
      J. Biol. Chem. 270:30384-30391(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-19, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    7. "The second step of lipid A biosynthesis, UDP-3-O-acyl-GlcNAc deacetylase is encoded by the pleotropic permeability/cell division gene envA of E.coli."
      Young K., Silver L.L., Bramhill D., Caceres C.A., Stachula S.A., Shelly S.E., Raetz C.R.H., Anderson M.S.
      FASEB J. 7:1268-1268(1993)
      Cited for: FUNCTION.
    8. "asmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC)."
      Kloser A.W., Laird M.W., Misra R.
      J. Bacteriol. 178:5138-5143(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS.
    9. "Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis."
      Sorensen P.G., Lutkenhaus J., Young K., Eveland S.S., Anderson M.S., Raetz C.R.
      J. Biol. Chem. 271:25898-25905(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
      Strain: K12.
    10. "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme."
      Jackman J.E., Raetz C.R., Fierke C.A.
      Biochemistry 38:1902-1911(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli."
      Ogura T., Inoue K., Tatsuta T., Suzaki T., Karata K., Young K., Su L.H., Fierke C.A., Jackman J.E., Raetz C.R., Coleman J., Tomoyasu T., Matsuzawa H.
      Mol. Microbiol. 31:833-844(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY FTSH PROTEASE, ENZYME REGULATION.
      Strain: K12 / W3110 and W2252.
    12. "Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site."
      Jackman J.E., Raetz C.R., Fierke C.A.
      Biochemistry 40:514-523(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-19; GLU-78; HIS-79; HIS-238; ASP-242; ASP-246 AND HIS-265.
    13. "UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism."
      Hernick M., Gennadios H.A., Whittington D.A., Rusche K.M., Christianson D.W., Fierke C.A.
      J. Biol. Chem. 280:16969-16978(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ACTIVE SITE.
    14. "The C-terminal end of LpxC is required for degradation by the FtsH protease."
      Fuehrer F., Langklotz S., Narberhaus F.
      Mol. Microbiol. 59:1025-1036(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY FTSH PROTEASE, ENZYME REGULATION, DOMAIN.
      Strain: K12.
    15. "Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis."
      Barb A.W., Zhou P.
      Curr. Pharm. Biotechnol. 9:9-15(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DRUG TARGET.
    16. "Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity."
      Hernick M., Gattis S.G., Penner-Hahn J.E., Fierke C.A.
      Biochemistry 49:2246-2255(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, MUTAGENESIS OF CYS-63.
    17. "Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions."
      Gattis S.G., Hernick M., Fierke C.A.
      J. Biol. Chem. 285:33788-33796(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    18. "Screening for antibacterial inhibitors of the UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) using a high-throughput mass spectrometry assay."
      Langsdorf E.F., Malikzay A., Lamarr W.A., Daubaras D., Kravec C., Zhang R., Hart R., Monsma F., Black T., Ozbal C.C., Miesel L., Lunn C.A.
      J. Biomol. Screen. 15:52-61(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DRUG TARGET.
    19. "Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria."
      Langklotz S., Schaekermann M., Narberhaus F.
      J. Bacteriol. 193:1090-1097(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY FTSH PROTEASE, ENZYME REGULATION.
    20. "FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp."
      Schaekermann M., Langklotz S., Narberhaus F.
      J. Bacteriol. 195:1912-1919(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY FTSH PROTEASE, ENZYME REGULATION.
    21. "Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer."
      Clayton G.M., Klein D.J., Rickert K.W., Patel S.B., Kornienko M., Zugay-Murphy J., Reid J.C., Tummala S., Sharma S., Singh S.B., Miesel L., Lumb K.J., Soisson S.M.
      J. Biol. Chem. 288:34073-34080(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH UDP-(3-O-(R-HYDROXYMYRISTOYL))-GLUCOSAMINE AND ZINC, ACTIVE SITE.
    22. "Structural basis of the promiscuous inhibitor susceptibility of Escherichia coli LpxC."
      Lee C.J., Liang X., Gopalaswamy R., Najeeb J., Ark E.D., Toone E.J., Zhou P.
      ACS Chem. Biol. 9:237-246(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITORS AND ZINC.

    Entry informationi

    Entry nameiLPXC_ECOLI
    AccessioniPrimary (citable) accession number: P0A725
    Secondary accession number(s): P07652
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 7, 2005
    Last modified: March 16, 2016
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Due to its important role in lipid A synthesis, LpxC is an attractive target for the development of new antibacterial agents to treat Gram-negative infections. Many potent LpxC inhibitors with a variety of chemical scaffolds and distinct antibiotic profiles have been discovered.3 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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

    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 one 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.