PPX_ECO57
ID PPX_ECO57 Reviewed; 513 AA.
AC P0AFL8; P29014; P76981;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Exopolyphosphatase {ECO:0000303|PubMed:16678853};
DE Short=ExopolyPase {ECO:0000305};
DE EC=3.6.1.11 {ECO:0000250|UniProtKB:P0AFL6};
GN Name=ppx; OrderedLocusNames=Z3765, ECs3364;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3] {ECO:0007744|PDB:2FLO}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-513, AND SUBUNIT.
RX PubMed=16678853; DOI=10.1016/j.jmb.2006.04.031;
RA Rangarajan E.S., Nadeau G., Li Y., Wagner J., Hung M.N., Schrag J.D.,
RA Cygler M., Matte A.;
RT "The structure of the exopolyphosphatase (PPX) from Escherichia coli
RT O157:H7 suggests a binding mode for long polyphosphate chains.";
RL J. Mol. Biol. 359:1249-1260(2006).
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:0000269|PubMed:16678853}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG57612.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36787.1; -; Genomic_DNA.
DR PIR; D91049; D91049.
DR PIR; H85893; H85893.
DR RefSeq; NP_311391.1; NC_002695.1.
DR RefSeq; WP_001121363.1; NZ_SWKA01000005.1.
DR PDB; 2FLO; X-ray; 2.20 A; A/B/C/D=2-513.
DR PDBsum; 2FLO; -.
DR AlphaFoldDB; P0AFL8; -.
DR SMR; P0AFL8; -.
DR STRING; 155864.EDL933_3658; -.
DR EnsemblBacteria; AAG57612; AAG57612; Z3765.
DR EnsemblBacteria; BAB36787; BAB36787; ECs_3364.
DR GeneID; 66673633; -.
DR GeneID; 914211; -.
DR KEGG; ece:Z3765; -.
DR KEGG; ecs:ECs_3364; -.
DR PATRIC; fig|386585.9.peg.3514; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; RISEGCY; -.
DR EvolutionaryTrace; P0AFL8; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Magnesium; Membrane;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..513
FT /note="Exopolyphosphatase"
FT /id="PRO_0000194300"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 20..31
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:2FLO"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:2FLO"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:2FLO"
FT TURN 197..201
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:2FLO"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:2FLO"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 399..410
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 429..444
FT /evidence="ECO:0007829|PDB:2FLO"
FT TURN 445..448
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:2FLO"
FT HELIX 480..494
FT /evidence="ECO:0007829|PDB:2FLO"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:2FLO"
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
