ID   PPX2_MYCTO              Reviewed;         319 AA.
AC   L7N5A6;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Exopolyphosphatase 2 {ECO:0000305};
DE            Short=ExopolyPase 2 {ECO:0000305};
DE            EC=3.6.1.11 {ECO:0000269|PubMed:25784702};
DE   AltName: Full=PPX2 {ECO:0000303|PubMed:25784702};
GN   Name=ppx2 {ECO:0000303|PubMed:25784702};
GN   OrderedLocusNames=MT1054 {ECO:0000312|EMBL:AAK45305.1};
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, ACTIVITY REGULATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=25784702; DOI=10.1128/mbio.02428-14;
RA   Chuang Y.M., Bandyopadhyay N., Rifat D., Rubin H., Bader J.S.,
RA   Karakousis P.C.;
RT   "Deficiency of the novel exopolyphosphatase Rv1026/PPX2 leads to metabolic
RT   downshift and altered cell wall permeability in Mycobacterium
RT   tuberculosis.";
RL   MBio 6:E02428-E02428(2015).
CC   -!- FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases
CC       orthophosphate processively from the ends of the polyP chain. Prefers
CC       long-chain length polyphosphates as substrates.
CC       {ECO:0000269|PubMed:25784702}.
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:25784702};
CC   -!- ACTIVITY REGULATION: Exopolyphosphatase activity is inhibited by ppGpp
CC       alarmones produced during the bacterial stringent response.
CC       {ECO:0000269|PubMed:25784702}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P96374}.
CC   -!- DISRUPTION PHENOTYPE: PPX2 deficiency leads to increased polyP levels,
CC       early bacterial growth arrest and reduced susceptibility to the first-
CC       line drug isoniazid, as well as increased bacterial survival during
CC       exposure to stress conditions and within macrophages. Mutant shows
CC       increased thickness of the cell wall and reduced drug permeability.
CC       {ECO:0000269|PubMed:25784702}.
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; AE000516; AAK45305.1; -; Genomic_DNA.
DR   PIR; E70623; E70623.
DR   RefSeq; WP_003405299.1; NZ_KK341227.1.
DR   AlphaFoldDB; L7N5A6; -.
DR   SMR; L7N5A6; -.
DR   PRIDE; L7N5A6; -.
DR   EnsemblBacteria; AAK45305; AAK45305; MT1054.
DR   GeneID; 45424998; -.
DR   KEGG; mtc:MT1054; -.
DR   PATRIC; fig|83331.31.peg.1131; -.
DR   HOGENOM; CLU_025908_1_2_11; -.
DR   InParanoid; L7N5A6; -.
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..319
FT                   /note="Exopolyphosphatase 2"
FT                   /id="PRO_0000440101"
SQ   SEQUENCE   319 AA;  33664 MW;  8BF72E61F9F1E4BE CRC64;
     MALTRVAAID CGTNSIRLLI ADVGAGLARG ELHDVHRETR IVRLGQGVDA TGRFAPEAIA
     RTRTALTDYA ELLTFHHAER VRMVATSAAR DVVNRDVFFA MTADVLGAAL PGSAAEVITG
     AEEAELSFRG AVGELGSAGA PFVVVDLGGG STEIVLGEHE VVASYSADIG CVRLTERCLH
     SDPPTLQEVS TARRLVRERL EPALRTVPLE LARTWVGLAG TMTTLSALAQ SMTAYDAAAI
     HLSRVPGADL LEVCQRLIGM TRKQRAALAP MHPGRADVIG GGAIVVEELA RELRERAGID
     QLTVSEHDIL DGIALSLAG