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Q9RB37

- UPPP_FLAJ1

UniProt

Q9RB37 - UPPP_FLAJ1

Protein

Undecaprenyl-diphosphatase

Gene

uppP

Organism
Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin By similarity.By similarity

    Catalytic activityi

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

    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

    BioCyciFJOH376686:GIXN-588-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Undecaprenyl-diphosphatase (EC:3.6.1.27)
    Alternative name(s):
    Bacitracin resistance protein
    Undecaprenyl pyrophosphate phosphatase
    Gene namesi
    Name:uppP
    Synonyms:bacA, upk
    Ordered Locus Names:Fjoh_0569
    OrganismiFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae)
    Taxonomic identifieri376686 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium
    ProteomesiUP000006694: Chromosome

    Subcellular locationi

    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 – 265265Undecaprenyl-diphosphatasePRO_0000151142Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi376686.Fjoh_0569.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei18 – 3821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei41 – 6121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei69 – 8921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei95 – 11521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei133 – 15321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei171 – 19121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei210 – 23021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei245 – 26521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UppP family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1968.
    HOGENOMiHOG000218356.
    KOiK06153.
    OMAiFNDAHAK.
    OrthoDBiEOG6QP13M.

    Family and domain databases

    HAMAPiMF_01006. Undec_diphosphatase.
    InterProiIPR003824. UppP.
    [Graphical view]
    PfamiPF02673. BacA. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00753. undec_PP_bacA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9RB37-1 [UniParc]FASTAAdd to Basket

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    MNTLQAIVLA VIEGITEFLP VSSTGHMIIA SSFFGIAHED FTKLFTIVIQ    50
    LGAILSVVVL YFKRFFQTLD FYFKLLVAFI PAVVLGLLLS DFIDGLLENP 100
    VTVAVSLLIG GLILLKVDEW FNNPNAAETS QKITYLQALK IGLFQCIAMI 150
    PGVSRSGASI VGGMSQKLSR TTAAEFSFFL AVPTMLGATV KKCYDYYKAG 200
    FELSHDQVNI LIIGNVVAFI VALLAIKTFI SFLTKNGFKV FGYYRIIAGI 250
    ILLLIHFFIH PLTII 265
    Length:265
    Mass (Da):29,118
    Last modified:May 1, 2000 - v1
    Checksum:i84A4BF72F6145B0F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169967 Genomic DNA. Translation: AAD50462.1.
    CP000685 Genomic DNA. Translation: ABQ03604.1.
    RefSeqiWP_012022660.1. NC_009441.1.
    YP_001192923.1. NC_009441.1.

    Genome annotation databases

    EnsemblBacteriaiABQ03604; ABQ03604; Fjoh_0569.
    GeneIDi5089515.
    KEGGifjo:Fjoh_0569.
    PATRICi21895401. VBIFlaJoh53613_0587.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169967 Genomic DNA. Translation: AAD50462.1 .
    CP000685 Genomic DNA. Translation: ABQ03604.1 .
    RefSeqi WP_012022660.1. NC_009441.1.
    YP_001192923.1. NC_009441.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 376686.Fjoh_0569.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ03604 ; ABQ03604 ; Fjoh_0569 .
    GeneIDi 5089515.
    KEGGi fjo:Fjoh_0569.
    PATRICi 21895401. VBIFlaJoh53613_0587.

    Phylogenomic databases

    eggNOGi COG1968.
    HOGENOMi HOG000218356.
    KOi K06153.
    OMAi FNDAHAK.
    OrthoDBi EOG6QP13M.

    Enzyme and pathway databases

    BioCyci FJOH376686:GIXN-588-MONOMER.

    Family and domain databases

    HAMAPi MF_01006. Undec_diphosphatase.
    InterProi IPR003824. UppP.
    [Graphical view ]
    Pfami PF02673. BacA. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00753. undec_PP_bacA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Transposon insertions in the Flavobacterium johnsoniae ftsX gene disrupt gliding motility and cell division."
      Kempf M.J., McBride M.J.
      J. Bacteriol. 182:1671-1679(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Novel features of the polysaccharide-digesting gliding bacterium Flavobacterium johnsoniae as revealed by genome sequence analysis."
      McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.
      Appl. Environ. Microbiol. 75:6864-6875(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17061 / DSM 2064 / UW101.

    Entry informationi

    Entry nameiUPPP_FLAJ1
    AccessioniPrimary (citable) accession number: Q9RB37
    Secondary accession number(s): A5FMG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 81 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3