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Database: UniProt
Entry: Q3SJZ7_THIDA
LinkDB: Q3SJZ7_THIDA
Original site: Q3SJZ7_THIDA 
ID   Q3SJZ7_THIDA            Unreviewed;       491 AA.
AC   Q3SJZ7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE            EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN   OrderedLocusNames=Tbd_1046 {ECO:0000313|EMBL:AAZ96999.1};
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ96999.1, ECO:0000313|Proteomes:UP000008291};
RN   [1] {ECO:0000313|EMBL:AAZ96999.1, ECO:0000313|Proteomes:UP000008291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ96999.1,
RC   ECO:0000313|Proteomes:UP000008291};
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC       {ECO:0000256|ARBA:ARBA00007125}.
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DR   EMBL; CP000116; AAZ96999.1; -; Genomic_DNA.
DR   RefSeq; WP_011311558.1; NC_007404.1.
DR   AlphaFoldDB; Q3SJZ7; -.
DR   STRING; 292415.Tbd_1046; -.
DR   KEGG; tbd:Tbd_1046; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_4; -.
DR   OrthoDB; 9793035at2; -.
DR   Proteomes; UP000008291; Chromosome.
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:SF14; EXOPOLYPHOSPHATASE; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000313|EMBL:AAZ96999.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008291}.
FT   DOMAIN          21..303
FT                   /note="Ppx/GppA phosphatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02541"
FT   DOMAIN          310..477
FT                   /note="Ppx/GppA phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21447"
SQ   SEQUENCE   491 AA;  53604 MW;  25BB8DA09FA7900E CRC64;
     MKSYDTLAAV DLGSNSFRLE VARVAGDQLY PLDSLKETVR LAAGLQDDKI LDGAARERAL
     ACLRRFGERL RGLPAEAVRC VGTSTLRVAR NADAFLAEAE AALGHPIEIV AGREEARLIY
     LGVAHSLPAS PDRRLVVDIG GGSTEFIVGH GLKPHERESL HLGCVHFSRR FFEQGAVSRA
     ALKAAELSAR AEVERIAHAF GRGNWQQAVG SSGTARALRD ILEQSGWSAG GITRDGLDRL
     RDALLAAGDV ERLELPGLSR DRRPVIAGGF AIMAGLFAEL GIEQMDVAET AMREGILYDL
     LGRFHADDMR EATVAEFARR YHVDAGQAER VGRTVLRLFA ATGREDDNDA RVLGWAARLH
     EIGLSVSHSG YHRHSAYILE NADMPGFSRT EQARLALLAR AQRGALTKVA AVAAGAVDER
     DRRAIWLLRQ AVILCRSRAD PRLAEVSAES TSKRFCLTLP PGWLEQRPLT QRALDDEIQH
     WQALGLKYVL G
//
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