ID   RNB_ECOUT               Reviewed;         644 AA.
AC   Q1RC77;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=UTI89_C1559;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE07037.1; -; Genomic_DNA.
DR   RefSeq; WP_000485005.1; NC_007946.1.
DR   AlphaFoldDB; Q1RC77; -.
DR   SMR; Q1RC77; -.
DR   PRIDE; Q1RC77; -.
DR   EnsemblBacteria; ABE07037; ABE07037; UTI89_C1559.
DR   KEGG; eci:UTI89_C1559; -.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
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; RNA-binding.
FT   CHAIN           1..644
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_1000063887"
FT   DOMAIN          561..643
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   644 AA;  72485 MW;  F4E8A68CFE16B83F CRC64;
     MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI
     IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV PDHPLLKDAI PCRAARGLNH
     EFKEGDWAVA EMRRHPLKGD RSFYAELTQY ITFGDDHFVP WWVTLARHNL EKEAPDGVAT
     EMLDEGLVRE DLTALDFVTI DSASTEDMDD ALFAKALPDG KLQLIVAIAD PTAWIAEGSK
     LDKAAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTFST DGTIEDNIEF
     FAATIESKAK LVYDQVSDWL ENTGDWQPES EAIAEQVRLL AQICQRRGEW RHNHALVFKD
     RLDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA ARVLRDKLGF GIYNVHMGFD
     PANADALAAL LKTHGLHVDA EEVLTLDGFC KLRRELDAQP TGFLDSRIRR FQSFAEISTE
     PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM
     AERDVGDWLY ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAVRDE
     LVCSQENGTV QIKGETAYKV TDVIDVTIAE VRMETRSIIA RPVA