ID   PPX_SALTY               Reviewed;         513 AA.
AC   P0A269; O86091;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=STM2502;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WRAY;
RA   Kim K.S., Fraley C.D., Kornberg A.;
RT   "Polyphosphate kinase (ppk) and exopolyphosphatase (ppx) genes in
RT   Salmonella typhimurium.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AF085682; AAC34891.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21396.1; -; Genomic_DNA.
DR   RefSeq; NP_461437.1; NC_003197.2.
DR   RefSeq; WP_001123330.1; NC_003197.2.
DR   AlphaFoldDB; P0A269; -.
DR   SMR; P0A269; -.
DR   STRING; 99287.STM2502; -.
DR   PaxDb; P0A269; -.
DR   EnsemblBacteria; AAL21396; AAL21396; STM2502.
DR   GeneID; 1254024; -.
DR   KEGG; stm:STM2502; -.
DR   PATRIC; fig|99287.12.peg.2641; -.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; RISEGCY; -.
DR   PhylomeDB; P0A269; -.
DR   BioCyc; SENT99287:STM2502-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
DR   GO; GO:0016462; F:pyrophosphatase activity; IBA:GO_Central.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Magnesium; Membrane; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..513
FT                   /note="Exopolyphosphatase"
FT                   /id="PRO_0000194305"
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