ID   PPX_SALTI               Reviewed;         513 AA.
AC   P0A270; O86091;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Exopolyphosphatase {ECO:0000250|UniProtKB:P0AFL6};
DE            Short=ExopolyPase {ECO:0000250|UniProtKB:P0AFL6};
DE            EC=3.6.1.11 {ECO:0000250|UniProtKB:P0AFL6};
GN   Name=ppx; OrderedLocusNames=STY2743, t0355;
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC       orthophosphate processively from the ends of the polyP chain.
CC       {ECO:0000250|UniProtKB:P0AFL6}.
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:0000250|UniProtKB:P0AFL6};
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; AL513382; CAD02704.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68074.1; -; Genomic_DNA.
DR   RefSeq; NP_457037.1; NC_003198.1.
DR   RefSeq; WP_001123330.1; NZ_WSUR01000007.1.
DR   AlphaFoldDB; P0A270; -.
DR   SMR; P0A270; -.
DR   STRING; 220341.gene:17586638; -.
DR   KEGG; stt:t0355; -.
DR   KEGG; sty:STY2743; -.
DR   PATRIC; fig|220341.7.peg.2781; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; RISEGCY; -.
DR   OrthoDB; 9793035at2; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.70.2260; -; 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   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Magnesium; Membrane.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..513
FT                   /note="Exopolyphosphatase"
FT                   /id="PRO_0000194304"
SQ   SEQUENCE   513 AA;  58145 MW;  02ACBA7895F2ED6D CRC64;
     MPIYDKSPRP QEFAAVDLGS NSFHMVIARV VDGAMQIIGR LKQRVHLADG LGADNKLSEE
     AMERGLSCLS LFAERLQGFS PSSVCIVGTH TLRQAQNAAD FLKRAEKVIP YPIEIISGNE
     EARLIFMGVE HTQPEKGRKL VIDIGGGSTE LVIGENFEPR LVESRRMGCV SFAQLYFPGG
     VINKENFQRA RMAAAQKLET LTWQYRIQGW NVAMGASGTI KAAHEVLLAL GEKDGFITPE
     RLDKLKSEVL KHRSFNALSL PGLSEERKAV FVPGLAILCG VFDALAIREL RLSDGALREG
     VLYEMEGRFR HQDVRSRTAK SLANQYNIDR EQARRVLETT MQMYEQWQAQ QPKLAHPQLE
     ALLRWAAMLH EVGLNINHSG LHRHSAYILQ HSDLPGFNQE QQMMMATLVR YHRKAIKLDD
     MPRFTLFKKK QYLPLIQLLR LGVLLNNQRQ ATTTPPTLRL TTDDSHWTLC FPHDWFSQNA
     LVLLDLEKEQ QYWEAVTGWR LNIEEESSPE IAA
//