PPX_VIBCH
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 25-MAY-2022, entry version 99.
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; Proteobacteria; 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; 57739437; -.
DR KEGG; vch:VC_0722; -.
DR PATRIC; fig|243277.26.peg.690; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; RISEGCY; -.
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:0016462; F:pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central.
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; 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