PPX_ECOL6
ID PPX_ECOL6 Reviewed; 513 AA.
AC P0AFL7; P29014; P76981;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=c3020;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81470.1; -; Genomic_DNA.
DR RefSeq; WP_001121363.1; NC_004431.1.
DR AlphaFoldDB; P0AFL7; -.
DR SMR; P0AFL7; -.
DR STRING; 199310.c3020; -.
DR PRIDE; P0AFL7; -.
DR EnsemblBacteria; AAN81470; AAN81470; c3020.
DR GeneID; 66673633; -.
DR KEGG; ecc:c3020; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; RISEGCY; -.
DR BioCyc; ECOL199310:C3020-MON; -.
DR Proteomes; UP000001410; 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_0000194301"
SQ SEQUENCE 513 AA; 58136 MW; 58E58E0F5D9FB9C3 CRC64;
MPIHDKSPRP QEFAAVDLGS NSFHMVIARV VDGAMQIIGR LKQRVHLADG LGPDNMLSEE
AMTRGLNCLS LFAERLQGFS PASVCIVGTH TLRQALNATD FLKRAEKVIP YPIEIISGNE
EARLIFMGVE HTQPEKGRKL VIDIGGGSTE LVIGENFEPI LVESRRMGCV SFAQLYFPGG
VINKENFQRA RMAAAQKLET LTWQFRIQGW NVAMGASGTI KAAHEVLMEM GEKDGIITPE
RLEKLVKEVL RHRNFASLSL PGLSEERKTV FVPGLAILCG VFDALAIREL RLSDGALREG
VLYEMEGRFR HQDVRSRTAS SLANQYHIDS EQARRVLDTT MQMYEQWREQ QPKLAHPQLE
ALLRWAAMLH EVGLNINHSG LHRHSAYILQ NSDLPGFNQE QQLMMATLVR YHRKAIKLDD
LPRFTLFKKK QFLPLIQLLR LGVLLNNQRQ ATTTPPTLTL ITDDSHWTLR FPHDWFSQNA
LVLLDLEKEQ EYWEGVAGWR LKIEEESTPE IAA