ID   RNC_BACSU               Reviewed;         249 AA.
AC   P51833; O31734;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Ribonuclease 3;
DE            EC=3.1.26.3;
DE   AltName: Full=Ribonuclease III;
DE            Short=RNase III;
GN   Name=rnc; Synonyms=rncS; OrderedLocusNames=BSU15930;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8654983; DOI=10.1016/0378-1119(96)00181-3;
RA   Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.;
RT   "The effect of Srb, a homologue of the mammalian SRP receptor alpha-
RT   subunit, on Bacillus subtilis growth and protein translocation.";
RL   Gene 172:17-24(1996).
RN   [2]
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   [3]
RP   FUNCTION IN RRNA PRECURSOR PROCESSING, FUNCTION IN PRE-SCRNA PROCESSING,
RP   FUNCTION AS AN RNASE, AND DISRUPTION PHENOTYPE.
RX   PubMed=11123676; DOI=10.1046/j.1365-2958.2000.02185.x;
RA   Herskovitz M.A., Bechhofer D.H.;
RT   "Endoribonuclease RNase III is essential in Bacillus subtilis.";
RL   Mol. Microbiol. 38:1027-1033(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=17576666; DOI=10.1093/nar/gkm460;
RA   Yao S., Blaustein J.B., Bechhofer D.H.;
RT   "Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an
RT   additional endonuclease cleavage site.";
RL   Nucleic Acids Res. 35:4464-4473(2007).
RN   [5]
RP   FUNCTION IN RRNA PRECURSOR PROCESSING, RNASE ACTIVITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=18363798; DOI=10.1111/j.1365-2958.2008.06207.x;
RA   Redko Y., Bechhofer D.H., Condon C.;
RT   "Mini-III, an unusual member of the RNase III family of enzymes, catalyses
RT   23S ribosomal RNA maturation in B. subtilis.";
RL   Mol. Microbiol. 68:1096-1106(2008).
RN   [6]
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).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=22412379; DOI=10.1371/journal.pgen.1002520;
RA   Durand S., Gilet L., Bessieres P., Nicolas P., Condon C.;
RT   "Three essential ribonucleases-RNase Y, J1, and III-control the abundance
RT   of a majority of Bacillus subtilis mRNAs.";
RL   PLoS Genet. 8:E1002520-E1002520(2012).
RN   [8]
RP   FUNCTION IN TYPE I TOXIN-ANTITOXIN BSRE/SR5 DEGRADATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168 / DB104;
RX   PubMed=26940229; DOI=10.1080/15476286.2016.1156288;
RA   Mueller P., Jahn N., Ring C., Maiwald C., Neubert R., Meissner C.,
RA   Brantl S.;
RT   "A multistress responsive type I toxin-antitoxin system: bsrE/SR5 from the
RT   B. subtilis chromosome.";
RL   RNA Biol. 13:511-523(2016).
CC   -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC       ribosomal RNA transcript to yield the immediate precursors to the large
CC       and small rRNAs (23S and 16S). Also processes pre-scRNA (the precursor
CC       of the signal recognition particle RNA). Probably also processes some
CC       mRNAs, and tRNAs when they are encoded in the rRNA operon
CC       (PubMed:22229825, PubMed:26940229, PubMed:11123676, PubMed:17576666,
CC       PubMed:18363798, PubMed:22412379). Probably processes pre-crRNA and
CC       tracrRNA of type II CRISPR loci if present in the organism (Probable).
CC       Involved in degradation of type I toxin-antitoxin system duplex RNAs
CC       (PubMed:22229825, PubMed:26940229). {ECO:0000269|PubMed:11123676,
CC       ECO:0000269|PubMed:17576666, ECO:0000269|PubMed:18363798,
CC       ECO:0000269|PubMed:22229825, ECO:0000269|PubMed:22412379,
CC       ECO:0000269|PubMed:26940229, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Essential. Depletion leads to the accumulation of
CC       30S precursor rRNA (PubMed:11123676), and alteration of levels of about
CC       11% of total transcripts (PubMed:22412379, PubMed:11123676,
CC       PubMed:18363798). Increased half-life of type I toxin-antitoxin system
CC       RNAs of BsrG/SR4 and toxin BsrE mRNA (note these strains must have an
CC       essential second-site suppressor to survive) (PubMed:22229825,
CC       PubMed:26940229). {ECO:0000269|PubMed:11123676,
CC       ECO:0000269|PubMed:18363798, ECO:0000269|PubMed:22229825,
CC       ECO:0000269|PubMed:22412379, ECO:0000269|PubMed:26940229}.
CC   -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR   EMBL; D64116; BAA10976.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13466.1; -; Genomic_DNA.
DR   PIR; B69693; B69693.
DR   RefSeq; NP_389475.1; NC_000964.3.
DR   RefSeq; WP_003232030.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P51833; -.
DR   SMR; P51833; -.
DR   STRING; 224308.BSU15930; -.
DR   PaxDb; 224308-BSU15930; -.
DR   EnsemblBacteria; CAB13466; CAB13466; BSU_15930.
DR   GeneID; 83885597; -.
DR   GeneID; 936169; -.
DR   KEGG; bsu:BSU15930; -.
DR   PATRIC; fig|224308.179.peg.1733; -.
DR   eggNOG; COG0571; Bacteria.
DR   InParanoid; P51833; -.
DR   OrthoDB; 9805026at2; -.
DR   PhylomeDB; P51833; -.
DR   BioCyc; BSUB:BSU15930-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd10845; DSRM_RNAse_III_family; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   NCBIfam; TIGR02191; RNaseIII; 1.
DR   PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR   PANTHER; PTHR11207; RIBONUCLEASE III; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW   rRNA processing; tRNA processing.
FT   CHAIN           1..249
FT                   /note="Ribonuclease 3"
FT                   /id="PRO_0000180375"
FT   DOMAIN          20..149
FT                   /note="RNase III"
FT   DOMAIN          175..244
FT                   /note="DRBM"
FT   REGION          218..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        79
FT                   /note="A -> P (in Ref. 1; BAA10976)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="S -> P (in Ref. 1; BAA10976)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="Q -> E (in Ref. 1; BAA10976)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="Q -> QLNPPYDSGGFQYVCRLI (in Ref. 1; BAA10976)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  28425 MW;  304F3B0BF5B7CCDC CRC64;
     MSKHSHYKDK KKFYKKVEQF KEFQERISVH FQNEKLLYQA FTHSSYVNEH RKKPYEDNER
     LEFLGDAVLE LTISRFLFAK YPAMSEGDLT KLRAAIVCEP SLVSLAHELS FGDLVLLGKG
     EEMTGGRKRP ALLADVFEAF IGALYLDQGL EPVESFLKVY VFPKINDGAF SHVMDFKSQL
     QEYVQRDGKG SLEYKISNEK GPAHNREFEA IVSLKGEPLG VGNGRSKKEA EQHAAQEALA
     KLQKHHTKQ
//