ID   PPX_PSEAI               Reviewed;         506 AA.
AC   Q9S605; Q9S647;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Exopolyphosphatase {ECO:0000303|PubMed:10224002};
DE            Short=ExopolyPase {ECO:0000305};
DE            EC=3.6.1.11 {ECO:0000269|PubMed:10224002};
GN   Name=ppx {ECO:0000303|PubMed:10224002};
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=8830;
RX   PubMed=10224002; DOI=10.1128/aem.65.5.2065-2071.1999;
RA   Zago A., Chugani S., Chakrabarty A.M.;
RT   "Cloning and characterization of polyphosphate kinase and
RT   exopolyphosphatase genes from Pseudomonas aeruginosa 8830.";
RL   Appl. Environ. Microbiol. 65:2065-2071(1999).
CC   -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC       orthophosphate processively from the ends of the polyP chain.
CC       {ECO:0000269|PubMed:10224002}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC         ChEBI:CHEBI:43474; EC=3.6.1.11;
CC         Evidence={ECO:0000269|PubMed:10224002};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AFL6};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AFL6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AFL6};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P0AFL6}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
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DR   EMBL; AF053463; AAD29107.1; -; Genomic_DNA.
DR   EMBL; AF087931; AAD29114.1; -; Genomic_DNA.
DR   RefSeq; WP_003096337.1; NZ_WOEG01000013.1.
DR   AlphaFoldDB; Q9S605; -.
DR   SMR; Q9S605; -.
DR   PATRIC; fig|287.1480.peg.605; -.
DR   eggNOG; COG0248; Bacteria.
DR   BRENDA; 3.6.1.11; 5087.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022371; Exopolyphosphatase.
DR   InterPro; IPR003695; Ppx_GppA.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR03706; exo_poly_only; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Membrane.
FT   CHAIN           1..506
FT                   /note="Exopolyphosphatase"
FT                   /id="PRO_0000440099"
SQ   SEQUENCE   506 AA;  56419 MW;  DC0FFCA88680E4C7 CRC64;
     MDLQSMPQKP AEAFPLIAAL DLGSNSFHLC LAKANIHGEV RILERLGEKV QLAAGLDEER
     NLSEEATQRG LDCLRRFAQF ISGMPQGSVR VVATNALREA RNRSDFIRRA EEVLGHPVEV
     ISGREEARLI YLGVANSMPD SGGRRLVSDI GGGSTEFIIG QGFESELRES LQMGCVSYTQ
     RYFRDGKITP ARYAQAYTAA RLELMGIENS LRRLGWQQAV GASGTIRAVA LAIKAGGHGN
     GEISPDGLAW LKRKVLKLGD VEKLDLEGIK PDRRTIFPAG LAILEAIFDA LELEQMVHSE
     GALREGVLYD LVGRHQHEDV RERTISSLMQ RYHVDPEQAS RVEAKALKVL AEVGDAWELN
     DELHRDLLSW GARVHEIGLD IAHYHYHKHG AYLIEHSDLA GFSRQDQQML SLLVRGHRRN
     IPADKLAEFA AEGDKLVRLC IVLRFAILFH HIRGTQEMPS VRLKAEPKSL SVTFPEGWLE
     ANPLTQADFA QEAEWLKRVG YSLNVR