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Database: UniProt
Entry: A0A160FMG6_9BURK
LinkDB: A0A160FMG6_9BURK
Original site: A0A160FMG6_9BURK 
ID   A0A160FMG6_9BURK        Unreviewed;       541 AA.
AC   A0A160FMG6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE            EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN   ORFNames=AYM40_14380 {ECO:0000313|EMBL:ANB73416.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73416.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB73416.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73416.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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:0000256|ARBA:ARBA00000209};
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC       {ECO:0000256|ARBA:ARBA00007125}.
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DR   EMBL; CP014578; ANB73416.1; -; Genomic_DNA.
DR   RefSeq; WP_063496806.1; NZ_CP014578.1.
DR   AlphaFoldDB; A0A160FMG6; -.
DR   STRING; 1804984.AYM40_14380; -.
DR   KEGG; buz:AYM40_14380; -.
DR   Proteomes; UP000076852; Chromosome 1.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022371; Exopolyphosphatase.
DR   InterPro; IPR048950; Ppx_GppA_C.
DR   InterPro; IPR003695; Ppx_GppA_N.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   NCBIfam; TIGR03706; exo_poly_only; 1.
DR   PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR   PANTHER; PTHR30005:SF0; RETROGRADE REGULATION PROTEIN 2; 1.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   Pfam; PF21447; Ppx-GppA_III; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT   DOMAIN          64..349
FT                   /note="Ppx/GppA phosphatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02541"
FT   DOMAIN          357..523
FT                   /note="Ppx/GppA phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21447"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  58715 MW;  8237AA9B76504AC7 CRC64;
     MASLNSAVGH KAPKAPSGYP APSASNAAAH ARMESAYSMA TTPQLLAAVD LGSNSFRLIV
     GRVEETDAGS QIYQVDALRE PVRLAAGLSR DKMLDRASQV RGWDALKRFG ERLRDFHPDH
     VRAVATNTLR IAKNAGEFLG EAQAALGFPI EVIAGREEAR LIYAGAAHSV PASAGKRLVV
     DIGGGSTEFI IGSHYTPIKM ESLYIGCVSH SRAFFPAGNV DEYTMRQAEL AAGREIQIIS
     AEYKKTGWEQ AIGSSGTARA LAELVEANGF NDAGVTHGIS RGGLERLKRA LIKAENVNRL
     KLVALKADRI PVLAGGLSIM MAVFDELGVD YVDTTDGALR LGVLYDLLGR SQHEDMRTVT
     AEGFMRRYGV DRAQAGRIGE LAVRFYDQFA EPDEERRAEN RMFLGWAAAL HEIGLSISHS
     AYHKHSAYIA SNADMPGFSR TDQARLAALV LGHAGKLGKL SQTREVEWPL LFCLRLAALL
     CRRRADVGLP GIAVAQVNGG YEVRLPNEWV ANNPLTDYSL IQEAAEWEKV GIPYRVVYTD
     D
//
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