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Database: UniProt
Entry: F6EJN6_HOYSD
LinkDB: F6EJN6_HOYSD
Original site: F6EJN6_HOYSD 
ID   F6EJN6_HOYSD            Unreviewed;       315 AA.
AC   F6EJN6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=exopolyphosphatase {ECO:0000256|ARBA:ARBA00012451};
DE            EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN   OrderedLocusNames=AS9A_0631 {ECO:0000313|EMBL:AEF39085.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39085.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF39085.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
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; CP002786; AEF39085.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6EJN6; -.
DR   STRING; 443218.AS9A_0631; -.
DR   KEGG; asd:AS9A_0631; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_1_4_11; -.
DR   OrthoDB; 9793035at2; -.
DR   Proteomes; UP000009235; Chromosome.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003695; Ppx_GppA_N.
DR   PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR   PANTHER; PTHR30005:SF0; RETROGRADE REGULATION PROTEIN 2; 1.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT   DOMAIN          18..305
FT                   /note="Ppx/GppA phosphatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02541"
SQ   SEQUENCE   315 AA;  33656 MW;  C83E28A43964D650 CRC64;
     MRLGVLDVGS NTVHLLMVDA HRGGHPTPMS STKAALRLAE QMDKNGDLTK KCADSLVTTV
     AEFSGIAQSS GCEELMAFAT SAVRDAKNSE AVLARVKEEA GVALEVLPGV EEARLTFLAV
     RRWYGWSAGR ILNLDIGGGS LEISTGIDED PDAAMSLPLG AGRLTRDWLP EDPPDRRRIA
     VLRDWLDAEL SDVAKQITET GRPDLVVATS KTFRSLARLT GAAPSSAGPR VKRTLTEAGL
     RQIIAFISRM TASDRAELEG VSSDRAPQIV AGALVAEAAM RALRIDTVDI CPWALREGLI
     LRKLDTGFGN GETGE
//
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