ID   RPPH_BARBK              Reviewed;         170 AA.
AC   P35640; A1URP2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=RNA pyrophosphohydrolase;
DE            EC=3.6.1.-;
DE   AltName: Full=(Di)nucleoside polyphosphate hydrolase;
DE   AltName: Full=Ap4A pyrophosphatase;
DE   AltName: Full=Invasion protein A;
DE   AltName: Full=Invasion-associated locus protein A;
GN   Name=rppH; Synonyms=ialA, invA, nudH; OrderedLocusNames=BARBAKC583_0325;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7890422; DOI=10.1128/iai.63.4.1552-1562.1995;
RA   Mitchell S.J., Minnick M.F.;
RT   "Characterization of a two-gene locus from Bartonella bacilliformis
RT   associated with the ability to invade human erythrocytes.";
RL   Infect. Immun. 63:1552-1562(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9880487; DOI=10.1074/jbc.274.3.1203;
RA   Conyers G.B., Bessman M.J.;
RT   "The gene, ialA, associated with the invasion of human erythrocytes by
RT   Bartonella bacilliformis, designates a nudix hydrolase active on
RT   dinucleoside 5'-polyphosphates.";
RL   J. Biol. Chem. 274:1203-1206(1999).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=10694402; DOI=10.1021/bi992458n;
RA   Conyers G.B., Wu G., Bessman M.J., Mildvan A.S.;
RT   "Metal requirements of a diadenosine pyrophosphatase from Bartonella
RT   bacilliformis: magnetic resonance and kinetic studies of the role of
RT   Mn2+.";
RL   Biochemistry 39:2347-2354(2000).
CC   -!- FUNCTION: Accelerates the degradation of transcripts by removing
CC       pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a
CC       more labile monophosphorylated state that can stimulate subsequent
CC       ribonuclease cleavage (By similarity). Catalyzes the hydrolysis of
CC       diadenosine tetra-, penta-, or hexa-phosphate with the departure of ATP
CC       as leaving group. Preferred substrate is Ap4A. Also acts on diguanosine
CC       tetra- and penta-phosphate at a lesser extent. Required with IalB for
CC       erythrocytes invasion. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 divalent metal ions. Zinc, magnesium or manganese.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L25276; AAA87326.1; -; Genomic_DNA.
DR   EMBL; CP000524; ABM45640.1; -; Genomic_DNA.
DR   PIR; I40045; I40045.
DR   RefSeq; WP_005766249.1; NC_008783.1.
DR   AlphaFoldDB; P35640; -.
DR   SMR; P35640; -.
DR   STRING; 360095.BARBAKC583_0325; -.
DR   EnsemblBacteria; ABM45640; ABM45640; BARBAKC583_0325.
DR   KEGG; bbk:BARBAKC583_0325; -.
DR   PATRIC; fig|360095.6.peg.309; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_0_5; -.
DR   OMA; PCVGIML; -.
DR   OrthoDB; 1345242at2; -.
DR   Proteomes; UP000000643; Chromosome.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   HAMAP; MF_00298; Nudix_RppH; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR022927; RppH.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Manganese; Reference proteome; Virulence; Zinc.
FT   CHAIN           1..170
FT                   /note="RNA pyrophosphohydrolase"
FT                   /id="PRO_0000056992"
FT   DOMAIN          11..164
FT                   /note="Nudix hydrolase"
FT   MOTIF           52..73
FT                   /note="Nudix box"
SQ   SEQUENCE   170 AA;  20081 MW;  6A8154205A5019C3 CRC64;
     MDTMVDFKTL PYRKGVGIVV FNREGQVWIG RRLITSSHTY AEVSKLWQFP QGGIDEGEEP
     LDAARRELYE ETGMRSVNLI KEVQDWFCYD FPQELIGHVL NNQYRGQMQK WFAFQFIGET
     SEIVINSPEN SNKAEFDQWK WINLEVLPSI VVSFKRHVYM KVVHEFRNII