ID   PRPE_BACSU              Reviewed;         244 AA.
AC   O31614;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase PrpE [asymmetrical];
DE            EC=3.6.1.17;
DE   AltName: Full=Ap4A hydrolase;
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase;
DE            Short=Diadenosine tetraphosphatase;
GN   Name=prpE; Synonyms=yjbP; OrderedLocusNames=BSU11630;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, AND INHIBITION.
RC   STRAIN=168;
RX   PubMed=12059787; DOI=10.1042/bj20011591;
RA   Iwanicki A., Herman-Antosiewicz A., Pierechod M., Seror S.J.,
RA   Obuchowski M.;
RT   "PrpE, a PPP protein phosphatase from Bacillus subtilis with unusual
RT   substrate specificity.";
RL   Biochem. J. 366:929-936(2002).
RN   [3]
RP   FUNCTION IN SPORE GERMINATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=16740944; DOI=10.1128/jb.01877-05;
RA   Hinc K., Nagorska K., Iwanicki A., Wegrzyn G., Seror S.J., Obuchowski M.;
RT   "Expression of genes coding for GerA and GerK spore germination receptors
RT   is dependent on the protein phosphatase PrpE.";
RL   J. Bacteriol. 188:4373-4383(2006).
CC   -!- FUNCTION: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP. Does not
CC       hydrolyze Ap2a or Ap6A. Also has an ATPase activity. Was shown to
CC       dephosphorylate phosphotyrosine but not phosphoserine or
CC       phosphothreonine from phosphorylated peptides. Involved in spore
CC       germination by controlling expression of genes coding for GerA and GerK
CC       receptors. {ECO:0000269|PubMed:16740944}.
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:0000269|PubMed:12059787};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:12059787};
CC       Note=Nickel. 100-fold less efficiency with manganese.
CC       {ECO:0000269|PubMed:12059787};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA.
CC   -!- SUBCELLULAR LOCATION: Forespore {ECO:0000269|PubMed:16740944}.
CC   -!- SIMILARITY: Belongs to the PrpE family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13020.1; -; Genomic_DNA.
DR   PIR; H69844; H69844.
DR   RefSeq; NP_389045.1; NC_000964.3.
DR   RefSeq; WP_003244765.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31614; -.
DR   SMR; O31614; -.
DR   STRING; 224308.BSU11630; -.
DR   PaxDb; O31614; -.
DR   PRIDE; O31614; -.
DR   DNASU; 936412; -.
DR   EnsemblBacteria; CAB13020; CAB13020; BSU_11630.
DR   GeneID; 936412; -.
DR   KEGG; bsu:BSU11630; -.
DR   PATRIC; fig|224308.179.peg.1252; -.
DR   eggNOG; COG0639; Bacteria.
DR   InParanoid; O31614; -.
DR   OMA; CNKLYRY; -.
DR   PhylomeDB; O31614; -.
DR   BioCyc; BSUB:BSU11630-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0042763; C:intracellular immature spore; IEA:UniProtKB-SubCell.
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   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Germination; GTP-binding; Hydrolase; Nickel; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..244
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT                   [asymmetrical]"
FT                   /id="PRO_0000297545"
SQ   SEQUENCE   244 AA;  27463 MW;  16C1FB1AFC92BB78 CRC64;
     MAYDIISDIH GCYDEMTALI QKLGYTIKNG VPVHEEGRVL VFAGDLTDRG PKSIEVIRFV
     AGAYEKGAVR YVPGNHCNKL YRYLKGNPVK VMHGLETTAA ELEELSKDEK KSVSEQFMKL
     YETAPLYDIL HNGELVVAHA GIRADDIGKY TRRVKDFVLY GDVTGETYPD GRPIRRDWAA
     AYNGKAWVVY GHTPVKEPRK VNRTINIDTG CVFGNQLTGF RFPEIETVSV PSSLPYDESR
     FRPI