RNM_SALTY
ID RNM_SALTY Reviewed; 293 AA.
AC O54453;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=5'-3' exoribonuclease Rnm {ECO:0000250|UniProtKB:P77766};
DE EC=3.1.13.- {ECO:0000250|UniProtKB:P77766};
DE AltName: Full=3',5'-nucleotide bisphosphate phosphatase {ECO:0000250|UniProtKB:P77766};
DE EC=3.1.3.97 {ECO:0000250|UniProtKB:P77766};
DE AltName: Full=RNase AM {ECO:0000250|UniProtKB:P77766};
GN Name=rnm {ECO:0000250|UniProtKB:P77766};
GN Synonyms=trpH {ECO:0000312|EMBL:AAB93886.1};
GN OrderedLocusNames=STM1721 {ECO:0000312|EMBL:AAL20639.1};
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 [GENOMIC DNA].
RA Yang W., Bai Q., Skrypka I., Zhao G., Somerville R.L.;
RT "The 5'-upstream regions of the trp operons of Escherichia coli and
RT Salmonella typhimurium contain divergently oriented, TrpR-controlled
RT transcriptional units.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- FUNCTION: Exoribonuclease that catalyzes the last steps of 5S, 16S and
CC 23S rRNA 5'-end maturation. Removes 3 nucleotides (nt) from the 5' end
CC of 5S, 16S and 23S rRNA precursors to generate the mature 5' ends. 5S
CC and 23S rRNA maturation occurs more efficiently and accurately on
CC ribosomal particles as compared to free RNA. Efficiently catalyzes the
CC hydrolysis of the 3'-phosphate from 3',5'-bis-phosphonucleotides as
CC well as the successive hydrolysis of 5'-phosphomononucleotides from the
CC 5'-end of short pieces of RNA and DNA, with no specificity toward the
CC identity of the nucleotide base. Is more efficient at hydrolyzing RNA
CC oligonucleotides than DNA oligonucleotides. This enzyme can also
CC hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency lower
CC than that of the corresponding single-stranded oligonucleotides.
CC {ECO:0000250|UniProtKB:P77766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3',5'-bisphosphate + H2O = a ribonucleoside
CC 5'-phosphate + phosphate; Xref=Rhea:RHEA:43532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:83402; EC=3.1.3.97;
CC Evidence={ECO:0000250|UniProtKB:P77766};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P77766};
CC -!- SIMILARITY: Belongs to the PHP family. TrpH/YciV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB93886.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; U92714; AAB93886.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20639.1; -; Genomic_DNA.
DR RefSeq; NP_460680.1; NC_003197.2.
DR RefSeq; WP_000500442.1; NC_003197.2.
DR AlphaFoldDB; O54453; -.
DR SMR; O54453; -.
DR STRING; 99287.STM1721; -.
DR PaxDb; O54453; -.
DR DNASU; 1253240; -.
DR EnsemblBacteria; AAL20639; AAL20639; STM1721.
DR GeneID; 1253240; -.
DR KEGG; stm:STM1721; -.
DR PATRIC; fig|99287.12.peg.1818; -.
DR HOGENOM; CLU_067347_0_0_6; -.
DR OMA; CTWGGAT; -.
DR PhylomeDB; O54453; -.
DR BioCyc; SENT99287:STM1721-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0097657; F:3',5'-nucleotide bisphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 3: Inferred from homology;
KW Exonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW Nucleotide-binding; Reference proteome; rRNA processing.
FT CHAIN 1..293
FT /note="5'-3' exoribonuclease Rnm"
FT /id="PRO_0000065640"
FT BINDING 17
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 49
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
SQ SEQUENCE 293 AA; 32396 MW; BBDAFC33743B4FF4 CRC64;
MGAALSDTNY AVIYDLHSHT TASDGLLTPE TLVHRAVEMR VGTLAITDHD TTAAIPAARE
EISRSGLALN LIPGVEISTV WENHEIHIVG LNIDIAHPAM RDFLAQQTER RQARGRLIAE
RLEKAHIPGA WEGALRLANG GAVTRGHFAR FLVECGKAAT MADVFKKYLA RGKTGYVPPQ
WCTIEQAIDV IHHSGGKAVL AHPGRYDLSA KWLKRLVAHF ADHHGDAMEV AQCQQSPNER
TQLATLARQH HLWASLGSDF HQPCPWIELG RKLWLPAGVE GVWQTWEQPQ ISQ
