Reviewed, UniProtKB/Swiss-Prot O31614 (PRPE_BACSU)

Names and origin

Protein names

Recommended name:
    Bis(5'-nucleosyl)-tetraphosphatase prpE [asymmetrical]
    EC=3.6.1.17
Alternative name(s):
    Ap4A hydrolase
    Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
      Short name=Diadenosine tetraphosphatase

Gene names

Name:	prpE
Synonyms:	yjbP
Ordered Locus Names:	BSU11630

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Asymmetrically hydrolyzes Ap4p to yield AMP and ATP. Does not hydrolyze Ap2a or Ap6A. Also has an ATPase activity. Was shown to dephosphorylate phosphotyrosine but not phosphoserine or phosphothreonine from phosphorylated peptides. Involved in spore germination by controlling expression of genes coding for gerA and gerK receptors. Ref.3
Catalytic activity	P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP. Ref.2
Cofactor	Nickel. 100-fold less efficiency with manganese. Ref.2
Enzyme regulation	Inhibited by EDTA. HAMAP MF_01443
Subcellular location	Forespore. Ref.3
Sequence similarities	Belongs to the prpE family.

Ontologies

Keywords
Biological process	Germination
Ligand	GTP-binding Nickel Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	intracellular immature spore Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Inferred from electronic annotation. Source: HAMAP nickel ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 244	244	Bis(5'-nucleosyl)-tetraphosphatase prpE [asymmetrical] HAMAP MF_01443		PRO_0000297545

Sequences

	Sequence		Length	Mass (Da)
	O31614-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 16C1FB1AFC92BB78	FASTA	244	27,463
	10 20 30 40 50 60 MAYDIISDIH GCYDEMTALI QKLGYTIKNG VPVHEEGRVL VFAGDLTDRG PKSIEVIRFV 70 80 90 100 110 120 AGAYEKGAVR YVPGNHCNKL YRYLKGNPVK VMHGLETTAA ELEELSKDEK KSVSEQFMKL 130 140 150 160 170 180 YETAPLYDIL HNGELVVAHA GIRADDIGKY TRRVKDFVLY GDVTGETYPD GRPIRRDWAA 190 200 210 220 230 240 AYNGKAWVVY GHTPVKEPRK VNRTINIDTG CVFGNQLTGF RFPEIETVSV PSSLPYDESR FRPI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"PrpE, a PPP protein phosphatase from Bacillus subtilis with unusual substrate specificity." Iwanicki A., Herman-Antosiewicz A., Pierechod M., Seror S.J., Obuchowski M. Biochem. J. 366:929-936(2002) [PubMed: 12059787] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, INHIBITION. Strain: 168.
[3]	"Expression of genes coding for GerA and GerK spore germination receptors is dependent on the protein phosphatase PrpE." Hinc K., Nagorska K., Iwanicki A., Wegrzyn G., Seror S.J., Obuchowski M. J. Bacteriol. 188:4373-4383(2006) [PubMed: 16740944] [Abstract] Cited for: FUNCTION IN SPORE GERMINATION, SUBCELLULAR LOCATION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB13020.1.
PIR	H69844.
RefSeq	NP_389045.1.
3D structure databases
ModBase	Search...
Protein family/group databases
PptaseDB	P3D0410142.
Genome annotation databases
GeneID	936412.
GenomeReviews	Gene locus BSU11630 in contig AL009126_GR.
KEGG	bsu:BSU11630.
NMPDR	fig|224308.1.peg.1164.
Organism-specific databases
SubtiList	BG13145. prpE. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O31614.
OMA	O31614. HCNKLYR.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1164-MON.
BRENDA	3.6.1.17. 150.
Family and domain databases
HAMAP	MF_01443. [Tree]
InterPro	IPR004843. M-pesterase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRPE_BACSU

Accession

Primary (citable) accession number: O31614

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)