ID   PPX_PSEAE               Reviewed;         506 AA.
AC   Q9ZN70;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Exopolyphosphatase {ECO:0000303|PubMed:10382967, ECO:0000303|PubMed:26576296};
DE            Short=ExopolyPase {ECO:0000303|PubMed:10382967};
DE            EC=3.6.1.11 {ECO:0000269|PubMed:10382967, ECO:0000269|PubMed:26576296};
DE   AltName: Full=Polyphosphate:ADP phosphotransferase {ECO:0000303|PubMed:26576296};
DE            Short=PolyP:ADP phosphotransferase {ECO:0000303|PubMed:26576296};
DE            EC=2.7.4.1 {ECO:0000269|PubMed:26576296};
GN   Name=ppx {ECO:0000303|PubMed:10382967}; OrderedLocusNames=PA5241;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10382967; DOI=10.1093/dnares/6.2.103;
RA   Miyake T., Shiba T., Kameda A., Ihara Y., Munekata M., Ishige K.,
RA   Noguchi T.;
RT   "The gene for an exopolyphosphatase of Pseudomonas aeruginosa.";
RL   DNA Res. 6:103-108(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   FUNCTION AS A PHOSPHATASE, FUNCTION AS A TRANSFERASE, CATALYTIC ACTIVITY,
RP   COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND
RP   MUTAGENESIS OF GLU-126; ASP-149; GLY-151; SER-154 AND GLU-156.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=26576296; DOI=10.1155/2015/404607;
RA   Beassoni P.R., Gallarato L.A., Boetsch C., Garrido M.N., Lisa A.T.;
RT   "Pseudomonas aeruginosa exopolyphosphatase is also a polyphosphate: ADP
RT   phosphotransferase.";
RL   Enzyme Res. 2015:404607-404607(2015).
CC   -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC       orthophosphate processively from the ends of the polyP chain
CC       (PubMed:10382967, PubMed:26576296). Has also polyphosphate:ADP
CC       phosphotransferase activity, catalyzing the production of ATP from ADP
CC       and polyP (PubMed:26576296). {ECO:0000269|PubMed:10382967,
CC       ECO:0000269|PubMed:26576296}.
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:10382967, ECO:0000269|PubMed:26576296};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC         Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1;
CC         Evidence={ECO:0000269|PubMed:26576296};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:26576296};
CC   -!- ACTIVITY REGULATION: Exopolyphosphatase activity is stimulated by
CC       NH(4)(+) and K(+). Phosphotransferase activity is insensitive to the
CC       addition of K(+) or NH(4)(+) ions. {ECO:0000269|PubMed:26576296}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.3 uM for polyP(75) {ECO:0000269|PubMed:26576296};
CC         KM=3.29 uM for polyP(65) {ECO:0000269|PubMed:26576296};
CC         KM=7.14 uM for polyP(45) {ECO:0000269|PubMed:26576296};
CC         KM=11.03 uM for polyP(25) {ECO:0000269|PubMed:26576296};
CC         Note=kcat is 57.02 sec(-1) for hydrolase activity with polyP(75) as
CC         substrate. kcat is 53.03 sec(-1) for hydrolase activity with
CC         polyP(65) as substrate. kcat is 41.23 sec(-1) for hydrolase activity
CC         with polyP(45) as substrate. kcat is 40.20 sec(-1) for hydrolase
CC         activity with polyP(25) as substrate. kcat is 3.93 sec(-1) for
CC         transferase activity with polyP(65) as substrate. kcat is 4.28
CC         sec(-1) for transferase activity with polyP(25) as substrate.
CC         {ECO:0000269|PubMed:26576296};
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   -!- DOMAIN: The catalytic activity is found in the N-terminal region formed
CC       by subdomains I and II. The peptide that connects subdomains II and III
CC       is also essential for activity. The C-terminal domain may be important
CC       for the recognition and/or interaction with long polyP chains.
CC       {ECO:0000269|PubMed:26576296}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
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DR   EMBL; AB022715; BAA74460.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG08626.1; -; Genomic_DNA.
DR   PIR; H82991; H82991.
DR   RefSeq; NP_253928.1; NC_002516.2.
DR   RefSeq; WP_003120380.1; NC_002516.2.
DR   AlphaFoldDB; Q9ZN70; -.
DR   SMR; Q9ZN70; -.
DR   STRING; 208964.PA5241; -.
DR   PaxDb; 208964-PA5241; -.
DR   GeneID; 877947; -.
DR   KEGG; pae:PA5241; -.
DR   PATRIC; fig|208964.12.peg.5493; -.
DR   PseudoCAP; PA5241; -.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   InParanoid; Q9ZN70; -.
DR   OrthoDB; 9793035at2; -.
DR   PhylomeDB; Q9ZN70; -.
DR   BioCyc; PAER208964:G1FZ6-5361-MONOMER; -.
DR   BRENDA; 3.6.1.11; 5087.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IDA:PseudoCAP.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IDA:PseudoCAP.
DR   GO; GO:0071977; P:bacterial-type flagellum-dependent swimming motility; IMP:PseudoCAP.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:PseudoCAP.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IDA:PseudoCAP.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IMP:PseudoCAP.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0009372; P:quorum sensing; IMP:PseudoCAP.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022371; Exopolyphosphatase.
DR   InterPro; IPR048950; Ppx_GppA_C.
DR   InterPro; IPR003695; Ppx_GppA_N.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   NCBIfam; TIGR03706; exo_poly_only; 1.
DR   PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR   PANTHER; PTHR30005:SF14; EXOPOLYPHOSPHATASE; 1.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   Pfam; PF21447; Ppx-GppA_III; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Magnesium; Membrane; Reference proteome;
KW   Transferase.
FT   CHAIN           1..506
FT                   /note="Exopolyphosphatase"
FT                   /id="PRO_0000194303"
FT   MUTAGEN         126
FT                   /note="E->A: Almost loss of hydrolase and transferase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:26576296"
FT   MUTAGEN         149
FT                   /note="D->A: Almost loss of hydrolase and transferase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:26576296"
FT   MUTAGEN         151
FT                   /note="G->A: Almost loss of hydrolase and transferase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:26576296"
FT   MUTAGEN         154
FT                   /note="S->A: Almost loss of hydrolase and transferase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:26576296"
FT   MUTAGEN         156
FT                   /note="E->A: Almost loss of hydrolase and transferase
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:26576296"
SQ   SEQUENCE   506 AA;  56419 MW;  91FDA10CFA04E1D4 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
     GELHRDLLSW GARVHEIGLD IAHYHYHKHG AYLIEHSDLA GFSRQDQQML SLLVRGHRRN
     IPADKLAEFA EEGDKLVRLC IVLRFAILFH HIRGTQEMPS VRLKAEPKSL SVTFPEGWLE
     ANPLTQADFA QEAEWLKRVG YSLNVR
//