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Protein

Exopolyphosphatase

Gene

ppx

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain (PubMed:10382967, PubMed:26576296). Has also polyphosphate:ADP phosphotransferase activity, catalyzing the production of ATP from ADP and polyP (PubMed:26576296).2 Publications

Catalytic activityi

(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.2 Publications
ATP + (phosphate)(n) = ADP + (phosphate)(n+1).1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Exopolyphosphatase activity is stimulated by NH4+ and K+. Phosphotransferase activity is insensitive to the addition of K+ or NH4+ ions.1 Publication

Kineticsi

kcat is 57.02 sec(-1) for hydrolase activity with polyP(75) as substrate. kcat is 53.03 sec(-1) for hydrolase activity with polyP(65) as substrate. kcat is 41.23 sec(-1) for hydrolase activity with polyP(45) as substrate. kcat is 40.20 sec(-1) for hydrolase activity with polyP(25) as substrate. kcat is 3.93 sec(-1) for transferase activity with polyP(65) as substrate. kcat is 4.28 sec(-1) for transferase activity with polyP(25) as substrate.1 Publication
  1. KM=1.30 µM for polyP(75)1 Publication
  2. KM=3.29 µM for polyP(65)1 Publication
  3. KM=7.14 µM for polyP(45)1 Publication
  4. KM=11.03 µM for polyP(25)1 Publication

    GO - Molecular functioni

    • exopolyphosphatase activity Source: PseudoCAP
    • polyphosphate kinase activity Source: UniProtKB-EC

    GO - Biological processi

    • bacterial-type flagellum-dependent swarming motility Source: PseudoCAP
    • bacterial-type flagellum-dependent swimming motility Source: PseudoCAP
    • cellular response to nitrogen starvation Source: PseudoCAP
    • cellular response to phosphate starvation Source: PseudoCAP
    • glycolipid biosynthetic process Source: PseudoCAP
    • pathogenesis Source: PseudoCAP
    • polyphosphate catabolic process Source: GO_Central
    • quorum sensing Source: PseudoCAP
    • single-species biofilm formation Source: PseudoCAP

    Keywordsi

    Molecular functionHydrolase, Transferase
    LigandMagnesium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exopolyphosphatase2 Publications (EC:3.6.1.112 Publications)
    Short name:
    ExopolyPase1 Publication
    Alternative name(s):
    Polyphosphate:ADP phosphotransferase1 Publication (EC:2.7.4.11 Publication)
    Short name:
    PolyP:ADP phosphotransferase1 Publication
    Gene namesi
    Name:ppx1 Publication
    Ordered Locus Names:PA5241
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA5241.

    Subcellular locationi

    Q9ZN70:
    • Cell membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi126E → A: Almost loss of hydrolase and transferase activities. 1 Publication1
    Mutagenesisi149D → A: Almost loss of hydrolase and transferase activities. 1 Publication1
    Mutagenesisi151G → A: Almost loss of hydrolase and transferase activities. 1 Publication1
    Mutagenesisi154S → A: Almost loss of hydrolase and transferase activities. 1 Publication1
    Mutagenesisi156E → A: Almost loss of hydrolase and transferase activities. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001943031 – 506ExopolyphosphataseAdd BLAST506

    Proteomic databases

    PaxDbiQ9ZN70.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi208964.PA5241.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZN70.
    SMRiQ9ZN70.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The catalytic activity is found in the N-terminal region formed by subdomains I and II. The peptide that connects subdomains II and III is also essential for activity. The C-terminal domain may be important for the recognition and/or interaction with long polyP chains.1 Publication

    Sequence similaritiesi

    Belongs to the GppA/Ppx family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C9X. Bacteria.
    COG0248. LUCA.
    HOGENOMiHOG000258672.
    InParanoidiQ9ZN70.
    KOiK01524.
    OMAiKLIRLCV.
    PhylomeDBiQ9ZN70.

    Family and domain databases

    InterProiView protein in InterPro
    IPR022371. Exopolyphosphatase.
    IPR003695. Ppx_GppA.
    IPR030673. PyroPPase_GppA_Ppx.
    PfamiView protein in Pfam
    PF02541. Ppx-GppA. 1 hit.
    PIRSFiPIRSF001267. Pyrophosphatase_GppA_Ppx. 1 hit.
    TIGRFAMsiTIGR03706. exo_poly_only. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9ZN70-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDLQSMPQKP AEAFPLIAAL DLGSNSFHLC LAKANIHGEV RILERLGEKV
    60 70 80 90 100
    QLAAGLDEER NLSEEATQRG LDCLRRFAQF ISGMPQGSVR VVATNALREA
    110 120 130 140 150
    RNRSDFIRRA EEVLGHPVEV ISGREEARLI YLGVANSMPD SGGRRLVSDI
    160 170 180 190 200
    GGGSTEFIIG QGFESELRES LQMGCVSYTQ RYFRDGKITP ARYAQAYTAA
    210 220 230 240 250
    RLELMGIENS LRRLGWQQAV GASGTIRAVA LAIKAGGHGN GEISPDGLAW
    260 270 280 290 300
    LKRKVLKLGD VEKLDLEGIK PDRRTIFPAG LAILEAIFDA LELEQMVHSE
    310 320 330 340 350
    GALREGVLYD LVGRHQHEDV RERTISSLMQ RYHVDPEQAS RVEAKALKVL
    360 370 380 390 400
    AEVGDAWELN GELHRDLLSW GARVHEIGLD IAHYHYHKHG AYLIEHSDLA
    410 420 430 440 450
    GFSRQDQQML SLLVRGHRRN IPADKLAEFA EEGDKLVRLC IVLRFAILFH
    460 470 480 490 500
    HIRGTQEMPS VRLKAEPKSL SVTFPEGWLE ANPLTQADFA QEAEWLKRVG

    YSLNVR
    Length:506
    Mass (Da):56,419
    Last modified:May 1, 1999 - v1
    Checksum:i91FDA10CFA04E1D4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB022715 Genomic DNA. Translation: BAA74460.1.
    AE004091 Genomic DNA. Translation: AAG08626.1.
    PIRiH82991.
    RefSeqiNP_253928.1. NC_002516.2.
    WP_003120380.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG08626; AAG08626; PA5241.
    GeneIDi877947.
    KEGGipae:PA5241.
    PATRICifig|208964.12.peg.5493.

    Similar proteinsi

    Entry informationi

    Entry nameiPPX_PSEAE
    AccessioniPrimary (citable) accession number: Q9ZN70
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 1999
    Last modified: October 25, 2017
    This is version 92 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families