ID   RNB_SALTY               Reviewed;         644 AA.
AC   Q8ZP54;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Exoribonuclease 2 {ECO:0000255|HAMAP-Rule:MF_01036};
DE            EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01036};
DE   AltName: Full=Exoribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
DE            Short=RNase II {ECO:0000255|HAMAP-Rule:MF_01036};
DE            Short=Ribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
GN   Name=rnb {ECO:0000255|HAMAP-Rule:MF_01036}; OrderedLocusNames=STM1702;
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).
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3' to 5' direction.
CC       {ECO:0000255|HAMAP-Rule:MF_01036}.
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_01036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01036}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01036}.
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DR   EMBL; AE006468; AAL20620.1; -; Genomic_DNA.
DR   RefSeq; NP_460661.1; NC_003197.2.
DR   RefSeq; WP_000485055.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZP54; -.
DR   SMR; Q8ZP54; -.
DR   STRING; 99287.STM1702; -.
DR   PaxDb; Q8ZP54; -.
DR   EnsemblBacteria; AAL20620; AAL20620; STM1702.
DR   GeneID; 1253221; -.
DR   KEGG; stm:STM1702; -.
DR   PATRIC; fig|99287.12.peg.1796; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   PhylomeDB; Q8ZP54; -.
DR   BioCyc; SENT99287:STM1702-MON; -.
DR   Proteomes; UP000001014; 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-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 2.
DR   HAMAP; MF_01036; RNase_II; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR040476; CSD2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR011804; RNase_II.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF17876; CSD2; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02062; RNase_B; 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="Exoribonuclease 2"
FT                   /id="PRO_0000166388"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72439 MW;  0CCAF4865A675A56 CRC64;
     MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI
     VAVIHTEKER ESAEPEELIE PFLTRFVGKV QGKNDRLSIV PDHPLLKDAI PCRAARGVQH
     EFKEGDWAVA EMRRHPLKGD RSFYADLTQY ITFADDHFVP WWVTLARHNL EKEAPNGVAT
     EMLDEGLERQ DLTALNFVTI DSASTEDMDD ALYAEELADG RLQLTVAIAD PTAWIAEGSK
     LDNTAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP ALACRMIIAA DGTIDDDIAF
     FAATIESKAK LAYDNVSDWL ENNGTWQPDN EGIAQQIRLL HRICLSRSEW RHHHALVFKD
     RPDYRFVLGE KGEVLDIVAE PRRIANRIVE ESMIAANLCA ARVLRDKLGF GIYNVHTGFD
     PANADALAAL LKTHGLHVDA EEVLTLEGFC KLRRELDAQP SGFLDSRIRR FQSFAEISTE
     PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGEAI ARPQEDITQQ MAERRRLNRM
     AERDVGDWLY ARFLNDKAGT NTRFAAEIID VSRGGMRVRL VDNGAIAFIP APFLHAVRDE
     LVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPAA