ID   PRPE_BACVZ              Reviewed;         249 AA.
AC   A7Z3F2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=RBAM_011640;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS73528.1; -; Genomic_DNA.
DR   RefSeq; WP_012117293.1; NC_009725.2.
DR   AlphaFoldDB; A7Z3F2; -.
DR   SMR; A7Z3F2; -.
DR   STRING; 326423.RBAM_011640; -.
DR   EnsemblBacteria; ABS73528; ABS73528; RBAM_011640.
DR   KEGG; bay:RBAM_011640; -.
DR   HOGENOM; CLU_023125_3_0_9; -.
DR   OMA; CNKLYRY; -.
DR   Proteomes; UP000001120; Chromosome.
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   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nickel; Nucleotide-binding.
FT   CHAIN           1..249
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT                   [asymmetrical]"
FT                   /id="PRO_1000024421"
SQ   SEQUENCE   249 AA;  28124 MW;  6E795F074F8086C8 CRC64;
     MAYDIISDIH GCYDEMIALM QKLGYEVKDG TPVHSEDRTL VFAGDLTDRG PKSVEVMRFV
     AKAYEKGAVR YVPGNHCNKL YRYLKGNPVK VMHGLETTAA ELKELSPADR TEVSRQFIRL
     YESAPLYDIL HNGDLVVAHA GIKADDIGKY SRKVKEFVLY GDITGETHPD GRPVRRDWAA
     AYEGKAWIVY GHTPVKRPRI VNRTINIDTG CVFGNQLTGF RFPEHETVSV ESSMPYDASR
     FREDHGRQA