RNC_BACSU
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 03-AUG-2022, entry version 138.
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; Firmicutes; 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; P51833; -.
DR PRIDE; P51833; -.
DR EnsemblBacteria; CAB13466; CAB13466; BSU_15930.
DR GeneID; 936169; -.
DR KEGG; bsu:BSU15930; -.
DR PATRIC; fig|224308.179.peg.1733; -.
DR eggNOG; COG0571; Bacteria.
DR InParanoid; P51833; -.
DR OMA; LTHKSCK; -.
DR PhylomeDB; P51833; -.
DR BioCyc; BSUB:BSU15930-MON; -.
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; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 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 PANTHER; PTHR11207; PTHR11207; 2.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR TIGRFAMs; TIGR02191; RNaseIII; 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
