ID   PPX_VIBCH               Reviewed;         500 AA.
AC   Q9KU08; O86074;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   27-MAR-2024, entry version 106.
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=VC_0722;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor Inaba 92A1552;
RA   Ogawa N., Fraley C., Kornberg A.;
RT   "The polyphosphate kinase and exopolyphosphatase genes of Vibrio
RT   cholerae.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF083928; AAC32884.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93887.1; ALT_INIT; Genomic_DNA.
DR   PIR; C82289; C82289.
DR   RefSeq; NP_230371.1; NC_002505.1.
DR   RefSeq; WP_000214489.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KU08; -.
DR   SMR; Q9KU08; -.
DR   STRING; 243277.VC_0722; -.
DR   DNASU; 2615731; -.
DR   EnsemblBacteria; AAF93887; AAF93887; VC_0722.
DR   GeneID; 69720523; -.
DR   KEGG; vch:VC_0722; -.
DR   PATRIC; fig|243277.26.peg.690; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
DR   GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.70.2260; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022371; Exopolyphosphatase.
DR   InterPro; IPR048950; Ppx_GppA_C.
DR   InterPro; IPR003695; Ppx_GppA_N.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   NCBIfam; TIGR03706; exo_poly_only; 1.
DR   PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR   PANTHER; PTHR30005:SF14; EXOPOLYPHOSPHATASE; 1.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   Pfam; PF21447; Ppx-GppA_III; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Magnesium; Membrane; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Exopolyphosphatase"
FT                   /id="PRO_0000194306"
FT   CONFLICT        456
FT                   /note="T -> P (in Ref. 1; AAC32884)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  56445 MW;  8AD7BE0C9CB380C1 CRC64;
     MTTVVSNARE IAAIDLGSNS FHMVVAKVVD QDLQLISRHK QRVRLAAGLD EQKNLDEESI
     QRGLECLAMF AERLQGFEPR NVRIAATHTL RQARNANLFI QRALDVLPFP IEIIPGSEEA
     RLIYLGVAHT QPQADSMLVV DIGGGSTEMI IGKGFEAELL NSKQMGCVNF TERYFANGKL
     SRKNFAQAIV ASEQKLESIA SKYRKKGWQM AFGSSGTIKA IHEVLIGQGH EDGLITFERL
     SKLIEKLCEW DSIDDLQLPG LTDDRKPVFA AGVAILSAIF HGLNIKEMHF SDGALREGLL
     YEMEDRFKYS DIRLRTTENL AAKHLVDLEH AAKVKGHARE FLAQVANELG LPEGSELCDL
     LEWGALLHEV GLSINLQGFH RHSAYILRHN NMAGFNSEQQ LVLSNLARFQ RKSLKLNELD
     DFSLFKKKHI IGLIRVLRLA IVVNGQRNDD PLPPLTLSAK DDEWRLECEQ PDWLENNKLL
     HADLQTEQEY WREVGWQLLF
//