ID   PPX1_MYCBO              Reviewed;         344 AA.
AC   P65787; A0A1R3XXP1; Q11161; X2BF85;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Exopolyphosphatase 1 {ECO:0000250|UniProtKB:P9WHV5};
DE            Short=ExopolyPase 1 {ECO:0000250|UniProtKB:P9WHV5};
DE            EC=3.6.1.11 {ECO:0000250|UniProtKB:P9WHV5};
GN   OrderedLocusNames=BQ2027_MB0507 {ECO:0000312|EMBL:SIT99102.1};
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC       orthophosphate processively from the ends of the polyP chain.
CC       {ECO:0000250|UniProtKB:P9WHV5}.
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:P9WHV5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHV5}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIT99102.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WHV5};
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DR   EMBL; LT708304; SIT99102.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003402419.1; NC_002945.4.
DR   AlphaFoldDB; P65787; -.
DR   SMR; P65787; -.
DR   GeneID; 45424458; -.
DR   PATRIC; fig|233413.5.peg.552; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003695; Ppx_GppA.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..344
FT                   /note="Exopolyphosphatase 1"
FT                   /id="PRO_0000194308"
FT   REGION          319..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  36550 MW;  2EB2369FBBE65226 CRC64;
     MRLGVLDVGS NTVHLLVVDA HRGGHPTPMS STKATLRLAE ATDSSGKITK RGADKLISTI
     DEFAKIAISS GCAELMAFAT SAVRDAENSE DVLSRVRKET GVELQALRGE DESRLTFLAV
     RRWYGWSAGR ILNLDIGGGS LEVSSGVDEE PEIALSLPLG AGRLTREWLP DDPPGRRRVA
     MLRDWLDAEL AEPSVTVLEA GSPDLAVATS KTFRSLARLT GAAPSMAGPR VKRTLTANGL
     RQLIAFISRM TAVDRAELEG VSADRAPQIV AGALVAEASM RALSIEAVEI CPWALREGLI
     LRKLDSEADG TALIESSSVH TSVRAVGGQP ADRNAANRSR GSKP