ID   PRPE_BACMK              Reviewed;         246 AA.
AC   A9VJS5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
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};
GN   OrderedLocusNames=BcerKBAB4_1112;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY42361.1; -; Genomic_DNA.
DR   RefSeq; WP_002086958.1; NC_010184.1.
DR   AlphaFoldDB; A9VJS5; -.
DR   SMR; A9VJS5; -.
DR   STRING; 315730.BcerKBAB4_1112; -.
DR   EnsemblBacteria; ABY42361; ABY42361; BcerKBAB4_1112.
DR   KEGG; bwe:BcerKBAB4_1112; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_023125_3_0_9; -.
DR   OMA; CNKLYRY; -.
DR   Proteomes; UP000002154; Chromosome.
DR   GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-UniRule.
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   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nickel.
FT   CHAIN           1..246
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT                   [asymmetrical]"
FT                   /id="PRO_1000145931"
SQ   SEQUENCE   246 AA;  28184 MW;  5C2FCA5F7DF67F92 CRC64;
     MKYDIIGDIH GCFQEFQDLT TKLGYSWDSG IPIHNAKRRL AFVGDITDRG PHSLRMIEIV
     WELVINRKDA YYAPGNHCNK LYRFFLGRNV TIAHGLETTV AEYEALPSNK QQIIKEKFIT
     LYEQSPLYHI LDEKNLTVCH AGIRQDYIGR QDKKVQTFVL YGDITGEKHP DGSPVRQDWA
     KEYKGETWIV YGHTPVNEPR FVNHTVNIDT GAVFGGKLTG LRYPELETVS VPSSLPFVPE
     KFRPIS