PPX_PSEAE
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 03-AUG-2022, entry version 110.
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; Proteobacteria; 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 / 1C /
RC 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 / 1C /
RC 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 / 1C /
RC 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=1.30 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 sec(-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; NZ_JAAGAW010000055.1.
DR AlphaFoldDB; Q9ZN70; -.
DR SMR; Q9ZN70; -.
DR STRING; 287.DR97_2612; -.
DR PaxDb; Q9ZN70; -.
DR PRIDE; Q9ZN70; -.
DR EnsemblBacteria; AAG08626; AAG08626; 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 OMA; RISEGCY; -.
DR PhylomeDB; Q9ZN70; -.
DR BioCyc; PAER208964:G1FZ6-5361-MON; -.
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:0016462; F:pyrophosphatase activity; IBA:GO_Central.
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 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; 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
