PPX1_MYCTU
ID PPX1_MYCTU Reviewed; 344 AA.
AC P9WHV5; A7UC78; I6WYJ1; 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 52.
DE RecName: Full=Exopolyphosphatase 1 {ECO:0000305};
DE Short=ExopolyPase 1 {ECO:0000305};
DE EC=3.6.1.11 {ECO:0000269|PubMed:22880033};
DE AltName: Full=MTB-PPX1 {ECO:0000303|PubMed:22880033};
GN Name=ppx1 {ECO:0000305|PubMed:22880033}; OrderedLocusNames=Rv0496;
GN ORFNames=MTCY20G9.22;
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 PROTEIN SEQUENCE OF 3-22, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-344.
RC STRAIN=H37Rv;
RA Kim H.Y., Wook G.W.;
RT "Cloning and characterization of exopolyphosphatase gene from Mycobacterium
RT tuberculosis H37Rv.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP 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 short-chain length polyphosphates as substrates. Can also hydrolyze ATP
CC and ADP substrates, but lacks GTPase activity. Cannot hydrolyze pppGpp
CC to ppGpp. {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:0000269|PubMed:22880033};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22880033};
CC Note=Can also use, to a lesser extent, Mg(2+) and Zn(2+).
CC {ECO:0000269|PubMed:22880033};
CC -!- ACTIVITY REGULATION: Exopolyphosphatase activity is inhibited by
CC (p)ppGpp alarmones produced during the bacterial stringent response.
CC {ECO:0000269|PubMed:22880033}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for polyP(14) {ECO:0000269|PubMed:22880033};
CC KM=12.1 uM for polyP(60) {ECO:0000269|PubMed:22880033};
CC KM=17.3 uM for polyP(130) {ECO:0000269|PubMed:22880033};
CC KM=6.1 mM for ATP {ECO:0000269|PubMed:22880033};
CC Vmax=11.0 umol/min/mg enzyme with polyP(14) as substrate
CC {ECO:0000269|PubMed:22880033};
CC Vmax=7.9 umol/min/mg enzyme with polyP(60) as substrate
CC {ECO:0000269|PubMed:22880033};
CC Vmax=6.6 umol/min/mg enzyme with polyP(130) as substrate
CC {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 10.2 sec(-1) with polyP(14) as substrate. kcat is 7.3
CC sec(-1) with polyP(60) as substrate. kcat is 6.7 sec(-1) with
CC polyP(130) as substrate. kcat is 1.9 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP43231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP43231.1; ALT_INIT; Genomic_DNA.
DR EMBL; EU045359; ABS89148.1; -; Genomic_DNA.
DR PIR; C70745; C70745.
DR RefSeq; NP_215010.3; NC_000962.3.
DR RefSeq; WP_003402419.1; NC_018143.2.
DR AlphaFoldDB; P9WHV5; -.
DR SMR; P9WHV5; -.
DR STRING; 83332.Rv0496; -.
DR PaxDb; P9WHV5; -.
DR DNASU; 887234; -.
DR GeneID; 45424458; -.
DR GeneID; 887234; -.
DR KEGG; mtu:Rv0496; -.
DR PATRIC; fig|83332.111.peg.545; -.
DR TubercuList; Rv0496; -.
DR eggNOG; COG0248; Bacteria.
DR OMA; YVPKIGL; -.
DR BRENDA; 3.6.1.11; 3445.
DR Proteomes; UP000001584; Chromosome.
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 Direct protein sequencing; Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..344
FT /note="Exopolyphosphatase 1"
FT /id="PRO_0000194307"
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
