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UniProtKB - P60472 (UPPS_ECOLI)

Entry version 145 (07 Oct 2020)
Sequence version 1 (16 Feb 2004)
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Protein

Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)

Gene

ispU

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

Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+2 PublicationsNote: Binds 2 magnesium ions per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Inhibited by bisphosphonates.1 Publication

<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

  1. KM=0.4 µM for FPP (at pH 7.5 and at 25 degrees Celsius)1 Publication
  2. KM=4.1 µM for IPP (at pH 7.5 and at 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei261
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi26Magnesium1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei31Substrate1 Publication1
    Binding sitei39Substrate1 Publication1
    Binding sitei43Substrate1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei69Required for continued chain elongation1
    Active sitei74Proton acceptorBy similarity1
    Binding sitei75Substrate1 Publication1
    Binding sitei77Substrate1 Publication1
    Sitei137Important for determining product length1
    Binding sitei194Substrate1 Publication1
    Metal bindingi199Magnesium1
    Metal bindingi213Magnesium1
    Binding sitei213Isopentenyl diphosphate1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    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 functionTransferase
    Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.5.1.31, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P60472

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...    SwissLipidsi    		SLP:000001809

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC:2.5.1.31)
    Alternative name(s):
    Ditrans,polycis-undecaprenylcistransferase
    Undecaprenyl diphosphate synthase
    Short name:
    UDS
    Undecaprenyl pyrophosphate synthase
    Short name:
    UPP synthase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ispU
    Synonyms:rth, uppS, yaeS
    Ordered Locus Names:b0174, JW0169
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    <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

    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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi26D → A: Great decrease in activity. 1 Publication1
    Mutagenesisi31W → F: Decrease in activity; reduced affinity for decaprenyl diphosphate substrate analog. 1 Publication1
    Mutagenesisi43H → A: Great decreases in the catalytic efficiency and the affinity for FPP and IPP. 1 Publication1
    Mutagenesisi62I → A: Formation predominantly of C(60) and C(65) polymers rather than the C(55) polymer. 1 Publication1
    Mutagenesisi69A → L: Produces shorter polymers. 1 Publication1
    Mutagenesisi71S → A: Decrease in activity. 1 Publication1
    Mutagenesisi73E → A: Slight decrease in activity. 2 Publications1
    Mutagenesisi74N → A: Decrease in activity. 1 Publication1
    Mutagenesisi75W → A or F: Decrease in activity; reduced affinity for decaprenyl diphosphate substrate analog. 2 Publications1
    Mutagenesisi77R → A: Decrease in activity. 1 Publication1
    Mutagenesisi81E → A: Slight decrease in activity. 1 Publication1
    Mutagenesisi91W → F: Decrease in affinity for IPP. 1 Publication1
    Mutagenesisi103H → A: No effect. 1 Publication1
    Mutagenesisi105V → A: Formation predominantly of C(60), C(65) and C(70) polymers rather than the C(55) polymer. 1 Publication1
    Mutagenesisi137L → A: Formation predominantly of a C(70) polymer rather than the C(55) polymer. 1 Publication1
    Mutagenesisi143A → V: No effect on polymer length. 1 Publication1
    Mutagenesisi149W → F: Decrease in affinity for IPP. 1 Publication1
    Mutagenesisi150D → A: Great decrease in affinity for the substrate. 1 Publication1
    Mutagenesisi190D → A: No effect. 1 Publication1
    Mutagenesisi198E → A: No effect. 1 Publication1
    Mutagenesisi199H → A: Great decreases in the catalytic efficiency and in the affinity for IPP; when associated with A-213. 1 Publication1
    Mutagenesisi207W → F: Decrease in affinity for both IPP and decaprenyl diphosphate substrate analog. 1 Publication1
    Mutagenesisi213E → A: Great decrease in activity; reduced affinity for IPP. Great decreases in the catalytic efficiency and in the affinity for IPP; when associated with A-199. 2 Publications1
    Mutagenesisi218D → A: Slight decrease in activity. 1 Publication1
    Mutagenesisi221W → F: Decrease in affinity for IPP. 1 Publication1
    Mutagenesisi223D → A: No effect. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL4295580

    Drug and drug target database

    More...    DrugBanki    		DB07404, (1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID
    DB07409, (1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID
    DB07426, [1-HYDROXY-2-(1,1':3',1''-TERPHENYL-3-YLOXY)ETHANE-1,1-DIYL]BIS(PHOSPHONIC ACID)
    DB07410, [2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACID
    DB07780, Farnesyl diphosphate
    DB04695, Farnesyl thiopyrophosphate
    DB04714, ISOPENTENYL PYROPHOSPHATE

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001236091 – 253Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)Add BLAST253

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P60472

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

    More...    PaxDbi    		P60472

    PRoteomics IDEntifications database

    More...    PRIDEi    		P60472

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    6 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260767, 417 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-48251N

    Protein interaction database and analysis system

    More...    IntActi    		P60472, 4 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0174

    <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

    1253
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...    SMRi    		P60472

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P60472

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni26 – 30Substrate binding5
    Regioni71 – 73Substrate bindingBy similarity3
    Regioni200 – 202Substrate binding3

    <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 UPP synthase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0020, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_038505_1_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P60472

    KEGG Orthology (KO)

    More...    KOi    		K00806

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P60472

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00475, Cis_IPPS, 1 hit

    Database of protein disorder

    More...    DisProti    		DP00516

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.1180.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01139, ISPT, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001441, UPP_synth-like
    IPR018520, UPP_synth-like_CS
    IPR036424, UPP_synth-like_sf

    The PANTHER Classification System

    More...    PANTHERi    		PTHR10291, PTHR10291, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01255, Prenyltransf, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF64005, SSF64005, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00055, uppS, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS01066, UPP_SYNTHASE, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P60472-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV 
            60         70         80         90        100
    RRAVSFAANN GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL 
           110        120        130        140        150
    HRHNVRLRII GDTSRFNSRL QERIRKSEAL TAGNTGLTLN IAANYGGRWD 
           160        170        180        190        200
    IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH VCMHELAPVD LVIRTGGEHR 
           210        220        230        240        250
    ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE RRFGGTEPGD 

    ETA
    Length:253
    Mass (Da):28,444
    Last modified:February 16, 2004 - 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:i73DC9534C14CA7B9
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAB08603 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    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
    		U70214 Genomic DNA Translation: AAB08603.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73285.1
    AP009048 Genomic DNA Translation: BAA77849.2

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		F64741

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414716.1, NC_000913.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73285; AAC73285; b0174
    BAA77849; BAA77849; BAA77849

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		944874

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0169
    eco:b0174

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|511145.12.peg.180

    <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
    		U70214 Genomic DNA Translation: AAB08603.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73285.1
    AP009048 Genomic DNA Translation: BAA77849.2
    PIRiF64741
    RefSeqiNP_414716.1, NC_000913.3

    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
    1JP3X-ray1.80A/B1-253[»]
    1UEHX-ray1.73A/B1-253[»]
    1V7UX-ray2.35A/B1-253[»]
    1X06X-ray1.90A1-253[»]
    1X07X-ray2.20A1-253[»]
    1X08X-ray1.90A1-253[»]
    1X09X-ray1.87A1-253[»]
    2E98X-ray1.90A/B1-253[»]
    2E99X-ray2.00A/B1-253[»]
    2E9AX-ray2.10A/B1-253[»]
    2E9CX-ray2.05A/B1-253[»]
    2E9DX-ray2.50A/B1-253[»]
    3QASX-ray1.70A/B1-253[»]
    3SGVX-ray1.61A/B1-253[»]
    3SGXX-ray2.45A/B1-253[»]
    3SH0X-ray1.84A/B1-253[»]
    3TH8X-ray2.11A/B1-253[»]
    3WYJX-ray2.10A/B1-253[»]
    4H2JX-ray1.81A/B1-253[»]
    4H2MX-ray1.78A/B1-253[»]
    4H2OX-ray2.14A/B1-253[»]
    4H38X-ray1.95A/B1-253[»]
    4H3AX-ray1.98A/B1-253[»]
    4H3CX-ray1.93A/B1-253[»]
    5CQBX-ray2.20A/B2-253[»]
    5CQJX-ray2.15A/B1-253[»]
    5ZHEX-ray2.18A/B1-253[»]
    SMRiP60472
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260767, 417 interactors
    DIPiDIP-48251N
    IntActiP60472, 4 interactors
    STRINGi511145.b0174

    Chemistry databases

    ChEMBLiCHEMBL4295580
    DrugBankiDB07404, (1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID
    DB07409, (1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID
    DB07426, [1-HYDROXY-2-(1,1':3',1''-TERPHENYL-3-YLOXY)ETHANE-1,1-DIYL]BIS(PHOSPHONIC ACID)
    DB07410, [2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACID
    DB07780, Farnesyl diphosphate
    DB04695, Farnesyl thiopyrophosphate
    DB04714, ISOPENTENYL PYROPHOSPHATE
    SwissLipidsiSLP:000001809

    Proteomic databases

    jPOSTiP60472
    PaxDbiP60472
    PRIDEiP60472

    Genome annotation databases

    EnsemblBacteriaiAAC73285; AAC73285; b0174
    BAA77849; BAA77849; BAA77849
    GeneIDi944874
    KEGGiecj:JW0169
    eco:b0174
    PATRICifig|511145.12.peg.180

    Organism-specific databases

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

    More...    EchoBASEi    		EB3113

    Phylogenomic databases

    eggNOGiCOG0020, Bacteria
    HOGENOMiCLU_038505_1_1_6
    InParanoidiP60472
    KOiK00806
    PhylomeDBiP60472

    Enzyme and pathway databases

    BioCyciEcoCyc:UPPSYN-MONOMER
    MetaCyc:UPPSYN-MONOMER
    BRENDAi2.5.1.31, 2026
    SABIO-RKiP60472

    Miscellaneous databases

    EvolutionaryTraceiP60472

    Protein Ontology

    More...    PROi    		PR:P60472

    Family and domain databases

    CDDicd00475, Cis_IPPS, 1 hit
    DisProtiDP00516
    Gene3Di3.40.1180.10, 1 hit
    HAMAPiMF_01139, ISPT, 1 hit
    InterProiView protein in InterPro
    IPR001441, UPP_synth-like
    IPR018520, UPP_synth-like_CS
    IPR036424, UPP_synth-like_sf
    PANTHERiPTHR10291, PTHR10291, 1 hit
    PfamiView protein in Pfam
    PF01255, Prenyltransf, 1 hit
    SUPFAMiSSF64005, SSF64005, 1 hit
    TIGRFAMsiTIGR00055, uppS, 1 hit
    PROSITEiView protein in PROSITE
    PS01066, UPP_SYNTHASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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 nameiUPPS_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: P60472
    Secondary accession number(s): P75668, Q47675, Q9R2E4
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: October 7, 2020
    This is version 145 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, Reference proteome

    Documents

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