ID RNB_ECO55 Reviewed; 644 AA.
AC B7L4C3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=EC55989_1448;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU97306.1; -; Genomic_DNA.
DR RefSeq; WP_000484984.1; NC_011748.1.
DR AlphaFoldDB; B7L4C3; -.
DR SMR; B7L4C3; -.
DR GeneID; 66674887; -.
DR KEGG; eck:EC55989_1448; -.
DR HOGENOM; CLU_002333_7_3_6; -.
DR Proteomes; UP000000746; 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; 2.40.50.640; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01036; RNase_II; 1.
DR InterPro; IPR011129; CSD.
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 NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02062; RNase_B; 1.
DR PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 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; Nucleic acid-binding proteins; 4.
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_1000149457"
FT DOMAIN 561..643
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 644 AA; 72491 MW; 36B16712CDF14394 CRC64;
MFQDNPLLAQ LKQQLHSQTP RAEGVVKATE KGFGFLEVDA QKSYFIPPPQ MKKVMHGDRI
IAVIHSEKER ESAEPEELVE PFLTRFVGKV QGKNDRLAIV PDHPLLKDAI PCRAARGLNH
EFKEGDWAVA EMRRHPLKGD RSFYAELTQY ITFGDDHFVP WWVTLARHNL EKEAPDGVAT
EMLDEGLVRE DLTALDFVTI DSASTEDMDD ALFAKALPDD KLQLIVAIAD PTAWIAEGSK
LDKAAKIRAF TNYLPGFNIP MLPRELSDDL CSLRANEVRP VLACRMTLSA DGTIEDNIEF
FAATIESKAK LVYDQVSDWL ENTGDWQPES EAIAEQVRLL AQICQRRGEW RHNHALVFKD
RPDYRFILGE KGEVLDIVAE PRRIANRIVE EAMIAANICA ARVLRDKLGF GIYNVHMGFD
PANADALAAL LKTHGLHVDA EEVLTLDGFC KLRRELDAQP TGFLDSRIRR FQSFAEISTE
PGPHFGLGLE AYATWTSPIR KYGDMINHRL LKAVIKGETA TRPQDEITVQ MAERRRLNRM
AERDVGDWLY ARFLKDKAGT DTRFAAEIVD ISRGGMRVRL VDNGAIAFIP APFLHAVRDE
LVCSQENGTV QIKGETVYKV TDVIDVTIAE VRMETRSIIA RPVA
//
