ID   RNPH_ACIBS              Reviewed;         238 AA.
AC   B0VMP4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Ribonuclease PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            Short=RNase PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000255|HAMAP-Rule:MF_00564};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000255|HAMAP-Rule:MF_00564}; OrderedLocusNames=ABSDF0051;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
CC   -!- FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an important
CC       role in tRNA 3'-end maturation. Removes nucleotide residues following
CC       the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of
CC       RNA molecules by using nucleoside diphosphates as substrates, but this
CC       may not be physiologically important. Probably plays a role in
CC       initiation of 16S rRNA degradation (leading to ribosome degradation)
CC       during starvation. {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:17343, Rhea:RHEA-
CC         COMP:17344, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:173114;
CC         EC=2.7.7.56; Evidence={ECO:0000255|HAMAP-Rule:MF_00564};
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU468230; CAO99466.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VMP4; -.
DR   SMR; B0VMP4; -.
DR   EnsemblBacteria; CAO99466; CAO99466; ABSDF0051.
DR   KEGG; abm:ABSDF0051; -.
DR   HOGENOM; CLU_050858_0_0_6; -.
DR   OMA; KGKGQGW; -.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd11362; RNase_PH_bact; 1.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55666; SSF55666; 1.
DR   TIGRFAMs; TIGR01966; RNasePH; 1.
DR   PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; RNA-binding; rRNA processing; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..238
FT                   /note="Ribonuclease PH"
FT                   /id="PRO_1000129309"
FT   BINDING         86
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT   BINDING         124..126
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
SQ   SEQUENCE   238 AA;  26296 MW;  EF3216AD4D0B0BE6 CRC64;
     MRIDQRALDQ LREVKITRNY TRYAEGSVLV EFGHTKVLCT ASIDNSVPRF LKGQGQGWVT
     AEYGMLPRST HSRCDREAAR GKQTGRTQEI QRLIGRSLRA MVDLKKLGEN TITIDCDVIQ
     ADGGTRTASI TGAAVALVDA MNVLLAQKKI KQDPLKGLVA AISVGMYQDE VLLDLCYEED
     SNCQTDLNVV MTQAGEFIEI QGTAEDKPFT RAQSNAMLEM AEKGIAELIK KQQEALGW