RNPH_SALTY
ID RNPH_SALTY Reviewed; 238 AA.
AC P0A2C3; P26155;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=STM3734;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-238.
RX PubMed=3882417; DOI=10.1111/j.1432-1033.1985.tb08693.x;
RA Neuhard J., Stauning E., Kelln R.A.;
RT "Cloning and characterization of the pyrE gene and of PyrE::Mud1 (Ap lac)
RT fusions from Salmonella typhimurium.";
RL Eur. J. Biochem. 146:597-603(1985).
CC -!- FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide
CC residues following the -CCA terminus of tRNA and adds nucleotides to
CC the ends of RNA molecules by using nucleoside diphosphates as
CC substrates.
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}.
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DR EMBL; AE006468; AAL22593.1; -; Genomic_DNA.
DR PIR; A21911; A21911.
DR RefSeq; NP_462634.1; NC_003197.2.
DR RefSeq; WP_001247078.1; NC_003197.2.
DR AlphaFoldDB; P0A2C3; -.
DR SMR; P0A2C3; -.
DR STRING; 99287.STM3734; -.
DR PaxDb; P0A2C3; -.
DR EnsemblBacteria; AAL22593; AAL22593; STM3734.
DR GeneID; 1255258; -.
DR KEGG; stm:STM3734; -.
DR PATRIC; fig|99287.12.peg.3950; -.
DR HOGENOM; CLU_050858_0_0_6; -.
DR OMA; KGKGQGW; -.
DR PhylomeDB; P0A2C3; -.
DR BioCyc; SENT99287:STM3734-MON; -.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
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; Reference proteome; RNA-binding; rRNA processing;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..238
FT /note="Ribonuclease PH"
FT /id="PRO_0000139935"
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"
FT CONFLICT 173..175
FT /note="CDL -> RDP (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 25269 MW; 19008C0C39A840E5 CRC64;
MRPAGRSANQ VRPVTLTRNY TKHAEGSVLV EFGDTKVLCT ASIEEGVPRF LKGQGQGWIT
AEYGMLPRAT HTRNAREAAK GKQGGRTMEI QRLIARALRA AVDLKTLGEF TITLDCDVIQ
ADGGTRTASI TGACVALADA LNKLVANGKL KTNPMKGMVA AVSVGIVNGE AICDLEYVED
SAAETDMNVV MTEDGRIIEV QGTAEGEPFS HEELLTLLAL ARGGIESIVA TQKAALEN
