PPX_ECOLI
ID PPX_ECOLI Reviewed; 513 AA.
AC P0AFL6; P29014; P76981;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Exopolyphosphatase {ECO:0000303|PubMed:8380170};
DE Short=ExopolyPase {ECO:0000305};
DE EC=3.6.1.11 {ECO:0000269|PubMed:8380170};
DE AltName: Full=Metaphosphatase;
GN Name=ppx {ECO:0000303|PubMed:8380170}; OrderedLocusNames=b2502, JW2487;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=8380170; DOI=10.1016/s0021-9258(18)54198-3;
RA Akiyama M., Crooke E., Kornberg A.;
RT "An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in
RT a polyphosphate operon.";
RL J. Biol. Chem. 268:633-639(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SIMILARITY TO GPPA.
RX PubMed=8212131; DOI=10.1016/0968-0004(93)90172-j;
RA Reizer J., Reizer A., Saier M.H. Jr., Bork B., Sander C.;
RT "Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase
RT belong to the sugar kinase/actin/hsp 70 superfamily.";
RL Trends Biochem. Sci. 18:247-248(1993).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9143103; DOI=10.1128/aem.63.5.1689-1695.1997;
RA Van Dien S.J., Keyhani S., Yang C., Keasling J.D.;
RT "Manipulation of independent synthesis and degradation of polyphosphate in
RT Escherichia coli for investigation of phosphate secretion from the cell.";
RL Appl. Environ. Microbiol. 63:1689-1695(1997).
RN [7]
RP ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24560923; DOI=10.1016/j.molcel.2014.01.012;
RA Gray M.J., Wholey W.Y., Wagner N.O., Cremers C.M., Mueller-Schickert A.,
RA Hock N.T., Krieger A.G., Smith E.M., Bender R.A., Bardwell J.C., Jakob U.;
RT "Polyphosphate is a primordial chaperone.";
RL Mol. Cell 53:689-699(2014).
RN [8] {ECO:0007744|PDB:1U6Z}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND MUTAGENESIS OF GLU-121; ASP-143; GLU-150 AND GLU-371.
RX PubMed=16905100; DOI=10.1016/j.str.2006.06.009;
RA Alvarado J., Ghosh A., Janovitz T., Jauregui A., Hasson M.S., Sanders D.A.;
RT "Origin of exopolyphosphatase processivity: fusion of an ASKHA
RT phosphotransferase and a cyclic nucleotide phosphodiesterase homolog.";
RL Structure 14:1263-1272(2006).
CC -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC orthophosphate processively from the ends of the polyP chain. Has a
CC strong preference for long-chain polyphosphates and has only weak
CC affinity for smaller size polyP of about 15 residues.
CC {ECO:0000269|PubMed:16905100, ECO:0000269|PubMed:8380170,
CC ECO:0000269|PubMed:9143103}.
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:16905100, ECO:0000269|PubMed:8380170,
CC ECO:0000269|PubMed:9143103};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8380170};
CC -!- ACTIVITY REGULATION: Activity is redox-regulated. Highly sensitive to
CC inactivation by oxidation (PubMed:24560923). Strongly stimulated by
CC potassium salts (PubMed:8380170). {ECO:0000269|PubMed:24560923,
CC ECO:0000269|PubMed:8380170}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:8380170};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16905100,
CC ECO:0000269|PubMed:8380170}.
CC -!- INTERACTION:
CC P0AFL6; P0AFL6: ppx; NbExp=2; IntAct=EBI-551996, EBI-551996;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8380170};
CC Peripheral membrane protein {ECO:0000305|PubMed:8380170}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant accumulates polyP.
CC {ECO:0000269|PubMed:24560923}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
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DR EMBL; L06129; AAA24415.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75555.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16390.1; -; Genomic_DNA.
DR PIR; A45333; A45333.
DR RefSeq; NP_416997.1; NC_000913.3.
DR RefSeq; WP_001121363.1; NZ_STEB01000011.1.
DR PDB; 1U6Z; X-ray; 1.90 A; A/B=1-513.
DR PDBsum; 1U6Z; -.
DR AlphaFoldDB; P0AFL6; -.
DR SMR; P0AFL6; -.
DR BioGRID; 4260594; 11.
DR BioGRID; 851309; 3.
DR DIP; DIP-29140N; -.
DR IntAct; P0AFL6; 9.
DR STRING; 511145.b2502; -.
DR jPOST; P0AFL6; -.
DR PaxDb; P0AFL6; -.
DR PRIDE; P0AFL6; -.
DR EnsemblBacteria; AAC75555; AAC75555; b2502.
DR EnsemblBacteria; BAA16390; BAA16390; BAA16390.
DR GeneID; 66673633; -.
DR GeneID; 946970; -.
DR KEGG; ecj:JW2487; -.
DR KEGG; eco:b2502; -.
DR PATRIC; fig|1411691.4.peg.4236; -.
DR EchoBASE; EB1375; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR InParanoid; P0AFL6; -.
DR OMA; RISEGCY; -.
DR PhylomeDB; P0AFL6; -.
DR BioCyc; EcoCyc:PPX-MON; -.
DR BioCyc; MetaCyc:PPX-MON; -.
DR BRENDA; 3.6.1.11; 2026.
DR EvolutionaryTrace; P0AFL6; -.
DR PRO; PR:P0AFL6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004309; F:exopolyphosphatase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016462; F:pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0006798; P:polyphosphate catabolic process; IMP:EcoCyc.
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 3D-structure; Cell membrane; Direct protein sequencing; Hydrolase;
KW Magnesium; Membrane; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8380170"
FT CHAIN 2..513
FT /note="Exopolyphosphatase"
FT /id="PRO_0000194299"
FT MUTAGEN 121
FT /note="E->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:16905100"
FT MUTAGEN 143
FT /note="D->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:16905100"
FT MUTAGEN 150
FT /note="E->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:16905100"
FT MUTAGEN 371
FT /note="E->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:16905100"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:1U6Z"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:1U6Z"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:1U6Z"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:1U6Z"
FT TURN 370..376
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 399..410
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 429..444
FT /evidence="ECO:0007829|PDB:1U6Z"
FT TURN 445..448
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:1U6Z"
FT HELIX 480..493
FT /evidence="ECO:0007829|PDB:1U6Z"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:1U6Z"
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
