ID   PPX1_MYCTO              Reviewed;         344 AA.
AC   P9WHV4; L0T3X7; P65786; Q11161;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Exopolyphosphatase 1 {ECO:0000303|PubMed:22132215};
DE            Short=ExopolyPase 1 {ECO:0000305};
DE            EC=3.6.1.11 {ECO:0000269|PubMed:22132215};
GN   Name=ppx {ECO:0000303|PubMed:22132215}; OrderedLocusNames=MT0516;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=22132215; DOI=10.1371/journal.pone.0028076;
RA   Thayil S.M., Morrison N., Schechter N., Rubin H., Karakousis P.C.;
RT   "The role of the novel exopolyphosphatase MT0516 in Mycobacterium
RT   tuberculosis drug tolerance and persistence.";
RL   PLoS ONE 6:E28076-E28076(2011).
CC   -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC       orthophosphate processively from the ends of the polyP chain. Required
CC       for long-term survival of M.tuberculosis in necrotic lung lesions.
CC       {ECO:0000269|PubMed:22132215}.
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:22132215};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHV5}.
CC   -!- DISRUPTION PHENOTYPE: Mutant exhibits elevated intracellular levels of
CC       polyP and increased expression of mprB, sigE and rel. Deficiency
CC       results in decelerated growth during logarithmic-phase in axenic
CC       cultures, tolerance to the cell wall-active drug isoniazid, a
CC       significant survival defect in activated human macrophages and reduced
CC       persistence in the lungs of guinea pigs. {ECO:0000269|PubMed:22132215}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44739.1; -; Genomic_DNA.
DR   PIR; C70745; C70745.
DR   RefSeq; WP_003402419.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHV4; -.
DR   SMR; P9WHV4; -.
DR   PRIDE; P9WHV4; -.
DR   EnsemblBacteria; AAK44739; AAK44739; MT0516.
DR   GeneID; 45424458; -.
DR   KEGG; mtc:MT0516; -.
DR   HOGENOM; CLU_025908_1_4_11; -.
DR   BRENDA; 3.6.1.11; 3445.
DR   Proteomes; UP000001020; 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   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..344
FT                   /note="Exopolyphosphatase 1"
FT                   /id="PRO_0000428116"
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