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Database: UniProt
Entry: P56123
LinkDB: P56123
Original site: P56123 
ID   RNR_HELPY               Reviewed;         644 AA.
AC   P56123;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895};
DE            Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
DE   AltName: Full=VacB protein homolog;
GN   Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB;
GN   OrderedLocusNames=HP_1248;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700392 / 26695, N6, and X47-2AL;
RX   PubMed=19043582; DOI=10.1371/journal.pone.0003810;
RA   Thibonnier M., Thiberge J.M., De Reuse H.;
RT   "Trans-translation in Helicobacter pylori: essentiality of ribosome rescue
RT   and requirement of protein tagging for stress resistance and competence.";
RL   PLoS ONE 3:E3810-E3810(2008).
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01895}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01895};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:19043582}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR   EMBL; AE000511; AAD08293.1; -; Genomic_DNA.
DR   PIR; H64675; H64675.
DR   RefSeq; NP_208040.1; NC_000915.1.
DR   RefSeq; WP_001161318.1; NC_018939.1.
DR   AlphaFoldDB; P56123; -.
DR   SMR; P56123; -.
DR   DIP; DIP-3252N; -.
DR   IntAct; P56123; 11.
DR   MINT; P56123; -.
DR   STRING; 85962.HP_1248; -.
DR   PaxDb; 85962-C694_06450; -.
DR   EnsemblBacteria; AAD08293; AAD08293; HP_1248.
DR   KEGG; hpy:HP_1248; -.
DR   PATRIC; fig|85962.47.peg.1340; -.
DR   eggNOG; COG0557; Bacteria.
DR   InParanoid; P56123; -.
DR   OrthoDB; 9764149at2; -.
DR   PhylomeDB; P56123; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR011805; RNase_R.
DR   PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..644
FT                   /note="Ribonuclease R"
FT                   /id="PRO_0000166404"
FT   DOMAIN          573..644
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
SQ   SEQUENCE   644 AA;  74163 MW;  960C62605A041EE4 CRC64;
     MQGFLRSLFF GVKKIPKPFA PLVEKGVLKE ALELKKDRYF LKEGFDIGKV EKVKDKAFFI
     SLAKNYPKDP LIKNLPPSFK TDALILCQIE CSKKRPIAFF KAALLNADHT MIAYLAKKNN
     QIVAIPFKEP FKKPVSLKHS QKSLLELPRH CVVKIDTKKR EISEILGALE DPLIDENLSL
     SLFDRVKDFS KDCLNLAQHY AQLKASDFKD RINYSHIPFI TIDPKDAKDF DDAIFYDQEK
     RVLFVAVADV SEFVPKHSSL DKEARVRGFS VYFPNSVYPM LPLSLSQGAC SLKAFEKRLA
     LVYEIPLDNL KNARLSQGVI EVRANCTYEE INHFLSANQS SLDKDLQQSL LGFLEMALKL
     KKERLKKGFN FNSFENKLYL NKEGRIEKIE TEKESDAHTL IEEAMLLANQ SSARLLDEHF
     HNKGIYRTHK EPSLEQQKRL YDKLFDYEIV RPKNMGFFPF LEHALKIAKE KSIEREVSRL
     IIKSQNLALY SPLQESHFGL GFASYTHFTS PIRRYSDLAL HRLLKELLFY QAKGCSYLLE
     ETPELCAELN ALQKKAALIE RDFIKRKFAR LALELLEKEF LGVVLEVKDW VVVGLKEFIG
     LKVLVKTNKV FKPLEKVRVT ITHADLILGQ VRGEITERIK EHVS
//
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