ID   RNR2_LACLA              Reviewed;         665 AA.
AC   Q02146; O34129; Q9CG96;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 3.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Ribonuclease R 2 {ECO:0000255|HAMAP-Rule:MF_01895};
DE            Short=RNase R 2 {ECO:0000255|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
DE   AltName: Full=VacB protein homolog 2;
GN   Name=rnr2 {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB2;
GN   OrderedLocusNames=LL1205; ORFNames=L25961;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-665.
RC   STRAIN=NCDO 2118;
RX   PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA   Delorme C., Ehrlich S.D., Renault P.;
RT   "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL   J. Bacteriol. 174:6571-6579(1992).
RN   [3]
RP   SEQUENCE REVISION TO 518-529.
RA   Delorme C., Goupil-Feuillerat N., Godon J.-J., Ehrlich S.D., Renault P.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 615-665.
RC   STRAIN=IL1403;
RX   PubMed=7687248; DOI=10.1128/jb.175.14.4391-4399.1993;
RA   Delorme C., Godon J.-J., Ehrlich S.D., Renault P.;
RT   "Gene inactivation in Lactococcus lactis: histidine biosynthesis.";
RL   J. Bacteriol. 175:4391-4399(1993).
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01895}.
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_01895};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR   EMBL; AE005176; AAK05303.1; -; Genomic_DNA.
DR   EMBL; U92974; AAB81900.1; -; Genomic_DNA.
DR   PIR; A45734; A45734.
DR   PIR; E86775; E86775.
DR   RefSeq; NP_267361.1; NC_002662.1.
DR   RefSeq; WP_010905825.1; NC_002662.1.
DR   AlphaFoldDB; Q02146; -.
DR   SMR; Q02146; -.
DR   STRING; 272623.L25961; -.
DR   PaxDb; Q02146; -.
DR   EnsemblBacteria; AAK05303; AAK05303; L25961.
DR   KEGG; lla:L25961; -.
DR   PATRIC; fig|272623.7.peg.1300; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_7_0_9; -.
DR   OMA; YRTHKEP; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 2.
DR   HAMAP; MF_01895; RNase_R; 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; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR011805; RNase_R.
DR   InterPro; IPR022967; S1_dom.
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   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02063; RNase_R; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..665
FT                   /note="Ribonuclease R 2"
FT                   /id="PRO_0000166407"
FT   DOMAIN          579..662
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
FT   CONFLICT        535
FT                   /note="H -> R (in Ref. 2; AAB81900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        629
FT                   /note="K -> T (in Ref. 2; AAB81900)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   665 AA;  75274 MW;  9504252DB5048C21 CRC64;
     MVQLSELASA LNQTESKGVF SKHPKGFGFV HPEDATDKTN DIYIGKNDTK FAMDGDKVTV
     KVTYPKTEKR GASGQITKIN ERAVVDTVGT YRSLSNRQVK ALGYKGRIEL YNDRISDTLY
     IKQPLSGVQE EDVVSLKITQ YPTNTKTFEG KITGIIGHKG EVGLDILEVL CAMKIPQEFS
     SETLAEAEAF SEKLTDSDLQ DREDYRNEIT YTIDGDDSKD LDDAIHVKKL SNWHFELGVH
     IADVSHYVTE GSSLDEEAYS RATSVYVTDR VVPMLPVKLS NNLCSLNEAQ ERLTMSCLME
     IDDKGKIVSY KISPSVIKTT YRMTYNNVNK MIHQGQEGHR EALENFFKIT DSIKVAVELH
     EILETMRKDR GMIEFDESEA KIILDEKGHP IEIVKRDRDT AERMIESFML MANETVALDF
     QKKKLPSLYR VHDNPKEKSF AKLMEAAANA GFSLNSDSHQ AINFFADEIK GTSSEKALTY
     QLRHTMSTAV YSEKNTKHFG LAATNYTHFT SPIRRYPDLI IHRLLHLYPS DHSNHTKDEW
     KERLPEIASH SSDMEHRAVV TERIIDAMKK AEYMSERIGE VYTGTITGLQ KFGIFVALDN
     TVEGLIRVPN LHTGTTEELE FDEEASIFKG KKSETVYQIG QEIKIRVIAA NKRKGTVDFE
     QIAPE