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UniProtKB - P60472 (UPPS_ECOLI)

Entry version 149 (02 Jun 2021)
Sequence version 1 (16 Feb 2004)
Previous versions | rss
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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_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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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_section">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_section">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_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:
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_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:ispU
Synonyms:rth, uppS, yaeS
Ordered Locus Names:b0174, JW0169
<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

<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

<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>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		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
DB07404, BPH-608
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_section">'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_section">'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

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P60472

<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

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_length">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_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.

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

BindingDBiP60472
ChEMBLiCHEMBL4295580
DrugBankiDB07409, (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
DB07404, BPH-608
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
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

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_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: February 16, 2004
Last sequence update: February 16, 2004
Last modified: June 2, 2021
This is version 149 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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