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A5IIP0

- UPPP_THEP1

UniProt

A5IIP0 - UPPP_THEP1

Protein

Undecaprenyl-diphosphatase

Gene

uppP

Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.UniRule annotation

    Catalytic activityi

    Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate.UniRule annotation

    GO - Molecular functioni

    1. undecaprenyl-diphosphatase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. dephosphorylation Source: InterPro
    2. peptidoglycan biosynthetic process Source: UniProtKB-KW
    3. regulation of cell shape Source: UniProtKB-KW
    4. response to antibiotic Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Enzyme and pathway databases

    BioCyciTPET390874:GHJI-34-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Undecaprenyl-diphosphataseUniRule annotation (EC:3.6.1.27UniRule annotation)
    Alternative name(s):
    Bacitracin resistance proteinUniRule annotation
    Undecaprenyl pyrophosphate phosphataseUniRule annotation
    Gene namesi
    Name:uppPUniRule annotation
    Ordered Locus Names:Tpet_0034
    OrganismiThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
    Taxonomic identifieri390874 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000006558: Chromosome

    Subcellular locationi

    Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 237237Undecaprenyl-diphosphatasePRO_1000062819Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi390874.Tpet_0034.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei38 – 5821HelicalUniRule annotationAdd
    BLAST
    Transmembranei65 – 8521HelicalUniRule annotationAdd
    BLAST
    Transmembranei92 – 11221HelicalUniRule annotationAdd
    BLAST
    Transmembranei126 – 14621HelicalUniRule annotationAdd
    BLAST
    Transmembranei166 – 18621HelicalUniRule annotationAdd
    BLAST
    Transmembranei191 – 21121HelicalUniRule annotationAdd
    BLAST
    Transmembranei217 – 23721HelicalUniRule annotationAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UppP family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1968.
    HOGENOMiHOG000218357.
    KOiK06153.
    OMAiNANEAVD.
    OrthoDBiEOG6QP13M.

    Family and domain databases

    HAMAPiMF_01006. Undec_diphosphatase.
    InterProiIPR003824. UppP.
    [Graphical view]
    PfamiPF02673. BacA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A5IIP0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLLLGIIQG LTEFLPVSSS GHLTLLSHLL KTDLNAYQTA VLHLGTLVSV    50
    VLFAFDGIRR SLRSWRIILN LIVSTIPAGV FGVLFEKQID QLFSSPRFLP 100
    LFFSVTALIL MFTRYSSSGE KRMENMSFLD ALLVGIAQLF ALFPGISRSG 150
    ITVSSLLFMK YRGEDALQYS FLMSIPVVLG AGILGLEKGN ITILAPIFAF 200
    LSGLFALYVL SRSVRSGKIW QFSYYCLFVA ILSYLVG 237
    Length:237
    Mass (Da):26,182
    Last modified:June 26, 2007 - v1
    Checksum:i6369CA37DF0ACC55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000702 Genomic DNA. Translation: ABQ46063.1.
    RefSeqiYP_001243639.1. NC_009486.1.

    Genome annotation databases

    EnsemblBacteriaiABQ46063; ABQ46063; Tpet_0034.
    GeneIDi5171587.
    KEGGitpt:Tpet_0034.
    PATRICi23942785. VBIThePet65348_0034.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000702 Genomic DNA. Translation: ABQ46063.1 .
    RefSeqi YP_001243639.1. NC_009486.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 390874.Tpet_0034.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ46063 ; ABQ46063 ; Tpet_0034 .
    GeneIDi 5171587.
    KEGGi tpt:Tpet_0034.
    PATRICi 23942785. VBIThePet65348_0034.

    Phylogenomic databases

    eggNOGi COG1968.
    HOGENOMi HOG000218357.
    KOi K06153.
    OMAi NANEAVD.
    OrthoDBi EOG6QP13M.

    Enzyme and pathway databases

    BioCyci TPET390874:GHJI-34-MONOMER.

    Family and domain databases

    HAMAPi MF_01006. Undec_diphosphatase.
    InterProi IPR003824. UppP.
    [Graphical view ]
    Pfami PF02673. BacA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

    Entry informationi

    Entry nameiUPPP_THEP1
    AccessioniPrimary (citable) accession number: A5IIP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3