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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-Experimental evidence at protein leveli

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

Catalytic activityi

(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl diphosphate.

Cofactori

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

Enzyme regulationi

Inhibited by bisphosphonates.1 Publication

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
    Active sitei261
    Metal bindingi26Magnesium1
    Binding sitei31Substrate1 Publication1
    Binding sitei39Substrate1 Publication1
    Binding sitei43Substrate1 Publication1
    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

    GO - Molecular functioni

    • di-trans,poly-cis-decaprenylcistransferase activity Source: EcoCyc
    • magnesium ion binding Source: EcoCyc
    • polyprenyltransferase activity Source: GO_Central

    GO - Biological processi

    • cell cycle Source: UniProtKB-KW
    • cell division Source: UniProtKB-KW
    • cell wall organization Source: UniProtKB-KW
    • Gram-negative-bacterium-type cell wall biogenesis Source: EcoCyc
    • peptidoglycan biosynthetic process Source: EcoCyc
    • polyprenol biosynthetic process Source: EcoCyc
    • regulation of cell shape Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:UPPSYN-MONOMER.
    ECOL316407:JW0169-MONOMER.
    MetaCyc:UPPSYN-MONOMER.
    BRENDAi2.5.1.31. 2026.

    Names & Taxonomyi

    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
    Gene namesi
    Name:ispU
    Synonyms:rth, uppS, yaeS
    Ordered Locus Names:b0174, JW0169
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13329. ispU.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoCyc
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001236091 – 253Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)Add BLAST253

    Proteomic databases

    PaxDbiP60472.
    PRIDEiP60472.

    Interactioni

    Subunit structurei

    Homodimer.6 Publications

    Protein-protein interaction databases

    BioGridi4260767. 393 interactors.
    DIPiDIP-48251N.
    IntActiP60472. 4 interactors.
    STRINGi511145.b0174.

    Structurei

    Secondary structure

    1253
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi15 – 17Combined sources3
    Beta strandi19 – 25Combined sources7
    Helixi28 – 34Combined sources7
    Helixi39 – 59Combined sources21
    Beta strandi63 – 68Combined sources6
    Helixi72 – 75Combined sources4
    Helixi83 – 90Combined sources8
    Helixi93 – 102Combined sources10
    Beta strandi106 – 111Combined sources6
    Helixi113 – 115Combined sources3
    Helixi118 – 131Combined sources14
    Beta strandi138 – 144Combined sources7
    Helixi147 – 164Combined sources18
    Helixi169 – 171Combined sources3
    Helixi174 – 178Combined sources5
    Turni182 – 185Combined sources4
    Beta strandi191 – 197Combined sources7
    Beta strandi204 – 206Combined sources3
    Helixi207 – 209Combined sources3
    Beta strandi213 – 216Combined sources4
    Helixi221 – 223Combined sources3
    Helixi226 – 239Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    DisProtiDP00516.
    ProteinModelPortaliP60472.
    SMRiP60472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60472.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni26 – 30Substrate binding5
    Regioni71 – 73Substrate bindingBy similarity3
    Regioni200 – 202Substrate binding3

    Sequence similaritiesi

    Belongs to the UPP synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CR3. Bacteria.
    COG0020. LUCA.
    HOGENOMiHOG000006054.
    InParanoidiP60472.
    KOiK00806.
    OMAiWAKLKNK.
    PhylomeDBiP60472.

    Family and domain databases

    CDDicd00475. Cis_IPPS. 1 hit.
    Gene3Di3.40.1180.10. 1 hit.
    HAMAPiMF_01139. ISPT. 1 hit.
    InterProiIPR001441. UPP_synth-like.
    IPR018520. UPP_synth-like_CS.
    [Graphical view]
    PANTHERiPTHR10291. PTHR10291. 1 hit.
    PfamiPF01255. Prenyltransf. 1 hit.
    [Graphical view]
    SUPFAMiSSF64005. SSF64005. 1 hit.
    TIGRFAMsiTIGR00055. uppS. 1 hit.
    PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    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
    Checksum:i73DC9534C14CA7B9
    GO

    Sequence cautioni

    The sequence AAB08603 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    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.

    Genome annotation databases

    EnsemblBacteriaiAAC73285; AAC73285; b0174.
    BAA77849; BAA77849; BAA77849.
    GeneIDi944874.
    KEGGiecj:JW0169.
    eco:b0174.
    PATRICi32115457. VBIEscCol129921_0180.

    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:
    PDBei
    RCSB PDBi
    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[»]
    DisProtiDP00516.
    ProteinModelPortaliP60472.
    SMRiP60472.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260767. 393 interactors.
    DIPiDIP-48251N.
    IntActiP60472. 4 interactors.
    STRINGi511145.b0174.

    Proteomic databases

    PaxDbiP60472.
    PRIDEiP60472.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73285; AAC73285; b0174.
    BAA77849; BAA77849; BAA77849.
    GeneIDi944874.
    KEGGiecj:JW0169.
    eco:b0174.
    PATRICi32115457. VBIEscCol129921_0180.

    Organism-specific databases

    EchoBASEiEB3113.
    EcoGeneiEG13329. ispU.

    Phylogenomic databases

    eggNOGiENOG4105CR3. Bacteria.
    COG0020. LUCA.
    HOGENOMiHOG000006054.
    InParanoidiP60472.
    KOiK00806.
    OMAiWAKLKNK.
    PhylomeDBiP60472.

    Enzyme and pathway databases

    BioCyciEcoCyc:UPPSYN-MONOMER.
    ECOL316407:JW0169-MONOMER.
    MetaCyc:UPPSYN-MONOMER.
    BRENDAi2.5.1.31. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP60472.
    PROiP60472.

    Family and domain databases

    CDDicd00475. Cis_IPPS. 1 hit.
    Gene3Di3.40.1180.10. 1 hit.
    HAMAPiMF_01139. ISPT. 1 hit.
    InterProiIPR001441. UPP_synth-like.
    IPR018520. UPP_synth-like_CS.
    [Graphical view]
    PANTHERiPTHR10291. PTHR10291. 1 hit.
    PfamiPF01255. Prenyltransf. 1 hit.
    [Graphical view]
    SUPFAMiSSF64005. SSF64005. 1 hit.
    TIGRFAMsiTIGR00055. uppS. 1 hit.
    PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiUPPS_ECOLI
    AccessioniPrimary (citable) accession number: P60472
    Secondary accession number(s): P75668, Q47675, Q9R2E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: November 2, 2016
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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