ID   PPX2_MYCTU              Reviewed;         319 AA.
AC   P96374; A0A089QQT2; F2GHB4; I6X033; Q7D8Z2;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Exopolyphosphatase 2 {ECO:0000305};
DE            Short=ExopolyPase 2 {ECO:0000305};
DE            EC=3.6.1.11 {ECO:0000250|UniProtKB:L7N5A6};
GN   Name=ppx2 {ECO:0000250|UniProtKB:L7N5A6};
GN   OrderedLocusNames=Rv1026 {ECO:0000312|EMBL:CCP43776.1};
GN   ORFNames=LH57_05600 {ECO:0000312|EMBL:AIR13763.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=H37Rv;
RX   PubMed=22880033; DOI=10.1371/journal.pone.0042561;
RA   Choi M.Y., Wang Y., Wong L.L., Lu B.T., Chen W.Y., Huang J.D., Tanner J.A.,
RA   Watt R.M.;
RT   "The two PPX-GppA homologues from Mycobacterium tuberculosis have distinct
RT   biochemical activities.";
RL   PLoS ONE 7:E42561-E42561(2012).
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 (By similarity). Can
CC       also hydrolyze ATP and ADP substrates, but lacks GTPase activity.
CC       Cannot hydrolyze pppGpp to ppGpp (PubMed:22880033).
CC       {ECO:0000250|UniProtKB:L7N5A6, ECO:0000269|PubMed:22880033}.
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:L7N5A6};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.6 mM for ATP {ECO:0000269|PubMed:22880033};
CC         Vmax=0.7 umol/min/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:22880033};
CC         Note=kcat is 4.4 sec(-1) with ATP as substrate.
CC         {ECO:0000269|PubMed:22880033};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22880033}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}.
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DR   EMBL; CP009480; AIR13763.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP43776.1; -; Genomic_DNA.
DR   RefSeq; NP_215542.1; NC_000962.3.
DR   RefSeq; WP_003405299.1; NZ_NVQJ01000018.1.
DR   AlphaFoldDB; P96374; -.
DR   SMR; P96374; -.
DR   STRING; 83332.Rv1026; -.
DR   PaxDb; P96374; -.
DR   PRIDE; P96374; -.
DR   DNASU; 886089; -.
DR   GeneID; 45424998; -.
DR   GeneID; 886089; -.
DR   KEGG; mtu:Rv1026; -.
DR   PATRIC; fig|83332.111.peg.1138; -.
DR   TubercuList; Rv1026; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_1_2_11; -.
DR   OMA; IGCVRMT; -.
DR   PhylomeDB; P96374; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016462; F:pyrophosphatase activity; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..319
FT                   /note="Exopolyphosphatase 2"
FT                   /id="PRO_0000440100"
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