PPX_SALTI
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 25-MAY-2022, entry version 95.
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; Proteobacteria; 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; 220341.16503720; -.
DR EnsemblBacteria; AAO68074; AAO68074; t0355.
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 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 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.
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