Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0A725 (LPXC_ECOLI)

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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi79Zinc; via tele nitrogenUniRule annotation2 Publications1
    Metal bindingi238Zinc; via tele nitrogenUniRule annotation2 Publications1
    Metal bindingi242ZincUniRule annotation2 Publications1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei265Proton donorUniRule annotation2 Publications1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    • lipid A biosynthetic process Source: EcoliWiki
    View the complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    Biological processLipid A biosynthesis, Lipid biosynthesis, Lipid metabolism
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:UDPACYLGLCNACDEACETYL-MONOMER
    MetaCyc:UDPACYLGLCNACDEACETYL-MONOMER

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi
    UPA00359;UER00478

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...    SwissLipidsi    		SLP:000001888

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:lpxC1 PublicationUniRule annotation
    Synonyms:asmB1 Publication, envA1 Publication
    Ordered Locus Names:b0096, JW0094
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...    EcoGenei    		EG10265 lpxC

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    View the complete GO annotation on QuickGO ...

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi19H → A: 1400-fold decrease in activity. 1 Publication1
    Mutagenesisi19H → Q: 90-fold decrease in activity. 1 Publication1
    Mutagenesisi19H → Y: 200-fold decrease in activity. 1 Publication1
    Mutagenesisi63C → A: Reduces level of inhibition by metal ions. 1 Publication1
    Mutagenesisi78E → A: 700-fold decrease in activity. 1 Publication1
    Mutagenesisi78E → Q: 3000-fold decrease in activity. 1 Publication1
    Mutagenesisi79H → A: 2300-fold decrease in activity. 1 Publication1
    Mutagenesisi79H → Q: 1200-fold decrease in activity. 1 Publication1
    Mutagenesisi238H → A: 1100-fold decrease in activity. 1 Publication1
    Mutagenesisi242D → A: 10-fold decrease in activity. 1 Publication1
    Mutagenesisi242D → Q: 2300-fold decrease in activity. 1 Publication1
    Mutagenesisi246D → A: 1800-fold decrease in activity. 1 Publication1
    Mutagenesisi265H → A: 3800-fold decrease in activity. 1 Publication1
    Mutagenesisi265H → Q: 5600-fold decrease in activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL5244

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001919291 – 305UDP-3-O-acyl-N-acetylglucosamine deacetylaseAdd BLAST305

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Degraded by FtsH.4 Publications

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A725

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P0A725

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A725

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4261858, 381 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-48045N

    Protein interaction database and analysis system

    More...    IntActi    		P0A725, 5 interactors

    STRING: functional protein association networks

    More...    STRINGi    		316385.ECDH10B_0078

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P0A725

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1305
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4IS9X-ray2.13A/B1-300[»]
    4ISAX-ray1.80A1-300[»]
    4MDTX-ray2.59A/B/C/D1-305[»]
    4MQYX-ray2.00A1-305[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P0A725

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P0A725

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the LpxC family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105C7C Bacteria
    COG0774 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000256663

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A725

    KEGG Orthology (KO)

    More...    KOi    		K02535

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A725

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.30.1700.10, 1 hit
    3.30.230.20, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00388 LpxC, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR020568 Ribosomal_S5_D2-typ_fold
    IPR004463 UDP-acyl_GlcNac_deAcase
    IPR011334 UDP-acyl_GlcNac_deAcase_C
    IPR015870 UDP-acyl_N-AcGlcN_deAcase_N

    The PANTHER Classification System

    More...    PANTHERi    		PTHR33694 PTHR33694, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF03331 LpxC, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF54211 SSF54211, 2 hits

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00325 lpxC, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCA439A00813463AB
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti50F → S in ASMB2/3; reduced activity. 1 Publication1
    Natural varianti210G → S in ASMB1; reduced activity. 1 Publication1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    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

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A28381 BVECEA

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414638.1, NC_000913.3
    WP_000595482.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73207; AAC73207; b0096
    BAB96664; BAB96664; BAB96664

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		944816

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0094
    eco:b0096

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2184

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
    		PDB 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
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261858, 381 interactors
    DIPiDIP-48045N
    IntActiP0A725, 5 interactors
    STRINGi316385.ECDH10B_0078

    Chemistry databases

    BindingDBiP0A725
    ChEMBLiCHEMBL5244
    SwissLipidsiSLP:000001888

    Proteomic databases

    jPOSTiP0A725
    PaxDbiP0A725
    PRIDEiP0A725

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73207; AAC73207; b0096
    BAB96664; BAB96664; BAB96664
    GeneIDi944816
    KEGGiecj:JW0094
    eco:b0096
    PATRICifig|1411691.4.peg.2184

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB0261
    EcoGeneiEG10265 lpxC

    Phylogenomic databases

    eggNOGiENOG4105C7C Bacteria
    COG0774 LUCA
    HOGENOMiHOG000256663
    InParanoidiP0A725
    KOiK02535
    PhylomeDBiP0A725

    Enzyme and pathway databases

    UniPathwayi
    UPA00359;UER00478

    BioCyciEcoCyc:UDPACYLGLCNACDEACETYL-MONOMER
    MetaCyc:UDPACYLGLCNACDEACETYL-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P0A725

    Family and domain databases

    Gene3Di3.30.1700.10, 1 hit
    3.30.230.20, 1 hit
    HAMAPiMF_00388 LpxC, 1 hit
    InterProiView protein in InterPro
    IPR020568 Ribosomal_S5_D2-typ_fold
    IPR004463 UDP-acyl_GlcNac_deAcase
    IPR011334 UDP-acyl_GlcNac_deAcase_C
    IPR015870 UDP-acyl_N-AcGlcN_deAcase_N
    PANTHERiPTHR33694 PTHR33694, 1 hit
    PfamiView protein in Pfam
    PF03331 LpxC, 1 hit
    SUPFAMiSSF54211 SSF54211, 2 hits
    TIGRFAMsiTIGR00325 lpxC, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLPXC_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A725
    Secondary accession number(s): P07652
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 7, 2005
    Last modified: January 16, 2019
    This is version 105 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again