ID   PRPE_GEOSW              Reviewed;         245 AA.
AC   C5D7A6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase PrpE [asymmetrical] {ECO:0000255|HAMAP-Rule:MF_01443};
DE            EC=3.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01443};
DE   AltName: Full=Ap4A hydrolase {ECO:0000255|HAMAP-Rule:MF_01443};
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase {ECO:0000255|HAMAP-Rule:MF_01443};
DE            Short=Diadenosine tetraphosphatase {ECO:0000255|HAMAP-Rule:MF_01443};
GN   Name=prpE {ECO:0000255|HAMAP-Rule:MF_01443}; OrderedLocusNames=GWCH70_0778;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_01443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP +
CC         2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; EC=3.6.1.17;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01443};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01443};
CC   -!- SIMILARITY: Belongs to the PrpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01443}.
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DR   EMBL; CP001638; ACS23664.1; -; Genomic_DNA.
DR   RefSeq; WP_012749463.1; NC_012793.1.
DR   AlphaFoldDB; C5D7A6; -.
DR   SMR; C5D7A6; -.
DR   STRING; 471223.GWCH70_0778; -.
DR   EnsemblBacteria; ACS23664; ACS23664; GWCH70_0778.
DR   KEGG; gwc:GWCH70_0778; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_023125_3_0_9; -.
DR   OMA; CNKLYRY; -.
DR   OrthoDB; 900869at2; -.
DR   GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   CDD; cd07423; MPP_Prp_like; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_01443; PrpE; 1.
DR   InterPro; IPR023937; Bis(5'-nucleosyl)-tetraP_PrpE.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041780; MPP_PrpE-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nickel; Nucleotide-binding.
FT   CHAIN           1..245
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT                   [asymmetrical]"
FT                   /id="PRO_1000215291"
SQ   SEQUENCE   245 AA;  27938 MW;  08E4A07F4729732A CRC64;
     MKIDIIGDIH GCYSEFVKLT KKLGYEWDSG IPLHPDGRKL GFVGDLTDRG PQSLQTVEVV
     YSLVERESAY YVPGNHCNKL YRFFLGRNVQ ITHGLETTVE EYRALPPSEQ AMIRKKFMRL
     YEAAPLYAQL DNGRLIIAHA GLRRDYIGRN DKKVQTFVLY GDITGETNPD GTPVRRDWAK
     RYKGSAWIVY GHTPVKQPRI INRTINIDTG CVFGGALTAF RYPEIETISV PSSLPYVPEK
     FRTFD