PPX1_MYCLE
ID PPX1_MYCLE Reviewed; 339 AA.
AC P54882; Q9CB53;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 99.
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=ML2434; ORFNames=B2168_C2_208;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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=AAA17230.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U00018; AAA17230.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583925; CAC31951.1; -; Genomic_DNA.
DR PIR; G87213; G87213.
DR PIR; S72894; S72894.
DR RefSeq; NP_302578.1; NC_002677.1.
DR RefSeq; WP_010908897.1; NC_002677.1.
DR AlphaFoldDB; P54882; -.
DR SMR; P54882; -.
DR STRING; 272631.ML2434; -.
DR PRIDE; P54882; -.
DR EnsemblBacteria; CAC31951; CAC31951; CAC31951.
DR KEGG; mle:ML2434; -.
DR PATRIC; fig|272631.5.peg.4674; -.
DR Leproma; ML2434; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_1_4_11; -.
DR OMA; YVPKIGL; -.
DR Proteomes; UP000000806; 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; Reference proteome.
FT CHAIN 1..339
FT /note="Exopolyphosphatase 1"
FT /id="PRO_0000194309"
FT REGION 315..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 36243 MW; F52DE129DF2B002A CRC64;
MRLGVLDVGS NTVHLLVVDA YRGGHPTPMS STKATLRMVE ATDSSGKITK RAADKLVSTI
GEFAKIAVSS GCAELMAFAT SAVREAGNSD DVLSRVRKET GVRLQVLRGV DESRLTFLAV
RRWFGWSAGR IINLDIGGGS LELSNGVDEE PEVALSLPLG AGRLTREWLP DDPPGRRRVA
MLRDWLDSEL SDASVTVLEA GKPDLAVATS KTFRSLARLT GAAPSAAGPR AKRALTVNGL
RQLIAFISRM TASDRAELEG ISTERAPQIV AGALVAEASM RALSIETVDI CPWALREGLI
LRKLDSEADG TALVQTSVRD TRGQEVDRNA ANRSRGDKT
