RNR_BACSU
ID RNR_BACSU Reviewed; 779 AA.
AC O32231;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
DE AltName: Full=VacB protein homolog;
GN Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB, yvaJ;
GN OrderedLocusNames=BSU33610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17369301; DOI=10.1128/jb.00062-07;
RA Shin J.H., Price C.W.;
RT "The SsrA-SmpB ribosome rescue system is important for growth of Bacillus
RT subtilis at low and high temperatures.";
RL J. Bacteriol. 189:3729-3737(2007).
RN [3]
RP FUNCTION IN TYPE I TOXIN-ANTITOXIN BSRG/SR4 DEGRADATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / DB104;
RX PubMed=22229825; DOI=10.1111/j.1365-2958.2011.07952.x;
RA Jahn N., Preis H., Wiedemann C., Brantl S.;
RT "BsrG/SR4 from Bacillus subtilis--the first temperature-dependent type I
RT toxin-antitoxin system.";
RL Mol. Microbiol. 83:579-598(2012).
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs (By
CC similarity). Involved in degradation of type I toxin-antitoxin system
CC bsrG/SR4 RNAs (PubMed:22229825). {ECO:0000255|HAMAP-Rule:MF_01895,
CC ECO:0000269|PubMed:22229825}.
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 -!- INDUCTION: Constitutively expressed, part of a 5 gene operon with
CC multiple promoters. Not ethanol-stress induced.
CC {ECO:0000269|PubMed:17369301}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:17369301). Increased
CC half-life of type I toxin-antitoxin system RNAs of BsrG/SR4
CC (PubMed:22229825). {ECO:0000269|PubMed:17369301,
CC ECO:0000269|PubMed:22229825}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR EMBL; AL009126; CAB15366.1; -; Genomic_DNA.
DR PIR; G70027; G70027.
DR RefSeq; NP_391241.1; NC_000964.3.
DR RefSeq; WP_003228386.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32231; -.
DR SMR; O32231; -.
DR STRING; 224308.BSU33610; -.
DR PaxDb; O32231; -.
DR PRIDE; O32231; -.
DR EnsemblBacteria; CAB15366; CAB15366; BSU_33610.
DR GeneID; 938644; -.
DR KEGG; bsu:BSU33610; -.
DR PATRIC; fig|224308.179.peg.3646; -.
DR eggNOG; COG0557; Bacteria.
DR InParanoid; O32231; -.
DR OMA; DWYEYRS; -.
DR PhylomeDB; O32231; -.
DR BioCyc; BSUB:BSU33610-MON; -.
DR Proteomes; UP000001570; 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-UniRule.
DR Gene3D; 2.40.50.140; -; 3.
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; 2.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
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 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..779
FT /note="Ribonuclease R"
FT /id="PRO_0000166396"
FT DOMAIN 628..708
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
FT REGION 709..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..779
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88750 MW; 45E5A54EC41F5EE5 CRC64;
MEKEAFMEKL LSFMKEEAYK PLTVQELEEM LNITEAEEFK ELVKALVALE EKGLIVRTRS
DRYGIPEKMN LIKGKISAHA KGFAFLLPED TSLSDVFIPP NELNTAMNGD IVMVRLNSQS
SGSRQEGTVI RILERAIQRV VGTYTETRNF GFVIPDDKKI TSDIFIPKNG KNGAAEGHKV
VVKLTSYPEG RMNAEGEVET ILGHKNDPGI DILSVIHKHG LPGEFPADAM EQASSTPDTI
DEKDLKDRRD LRDQVIVTID GADAKDLDDA VTVTKLDDGS YKLGVHIADV SHYVTENSPI
DKEALERGTS VYLVDRVIPM IPHRLSNGIC SLNPKVDRLT LSCEMTINSQ GQVTEHEIFQ
SVIKTTERMT YSDVNKILVD DDEELKQKYE PLVPMFKDME RLAQILRDKR MDRGAVDFDF
KEAKVLVDDE GAVKDVVIRE RSVAEKLIEE FMLVANETVA EHFHWMNVPF IYRIHEEPNA
EKLQKFLEFV TTFGYVVKGT AGNIHPRALQ SILDAVRDRP EETVISTVML RSMKQAKYDP
QSLGHFGLST EFYTHFTSPI RRYPDLIVHR LIRTYLINGK VDEATQEKWA ERLPDIAEHT
SSMERRAVDA ERETDDLKKA EYMLDKIGEE FDGMISSVTN FGMFVELPNT IEGLVHVSFM
TDDYYRFDEQ HFAMIGERTG NVFRIGDEIT VKVVDVNKDE RNIDFEIVGM KGTPRRPREL
DSSRSRKRGK PARKRVQSTN TPVSPAPSEE KGEWFTKPKK KKKKRGFQNA PKQKRKKKK
