MRNC_BACSU
ID MRNC_BACSU Reviewed; 143 AA.
AC O31418;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Mini-ribonuclease 3;
DE Short=Mini-3;
DE Short=Mini-RNase 3;
DE EC=3.1.26.-;
DE AltName: Full=Mini-RNase III;
DE Short=Mini-III;
GN Name=mrnC; Synonyms=yazC; OrderedLocusNames=BSU00950;
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 DISCUSSION OF POSSIBLE FUNCTION.
RX PubMed=16014871; DOI=10.1093/molbev/msi211;
RA Fang G., Rocha E., Danchin A.;
RT "How essential are nonessential genes?";
RL Mol. Biol. Evol. 22:2147-2156(2005).
RN [3]
RP FUNCTION IN 23S RRNA PROCESSING, RNASE ACTIVITY, SUBUNIT, COFACTOR, AND
RP DISRUPTION 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 [4]
RP STIMULATION BY RPLC (RIBOSOMAL PROTEIN L3), AND MUTAGENESIS OF ASP-23 AND
RP 41-ARG--ASN-43.
RX PubMed=19154332; DOI=10.1111/j.1365-2958.2008.06591.x;
RA Redko Y., Condon C.;
RT "Ribosomal protein L3 bound to 23S precursor rRNA stimulates its maturation
RT by Mini-III ribonuclease.";
RL Mol. Microbiol. 71:1145-1154(2009).
CC -!- FUNCTION: Involved in correct processing of both the 5' and 3' ends of
CC 23S rRNA precursor. Processes 30S rRNA precursor transcript even in
CC absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller
CC rRNA precursors. Cleaves more efficiently on assembled 50S ribosomal
CC subunits. Cleavage is strongly stimulated by ribosomal protein L3
CC (RplC); 20-30% DMSO can replace RplC, suggesting RplC may alter rRNA
CC conformation. {ECO:0000269|PubMed:18363798}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18363798};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:18363798}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells accumulate precursors and mature forms of
CC 23S rRNA with alternative 5' and 3' ends. Defects are more marked
CC during exponential growth. {ECO:0000269|PubMed:18363798}.
CC -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000305}.
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DR EMBL; AL009126; CAB11871.1; -; Genomic_DNA.
DR PIR; C69742; C69742.
DR RefSeq; NP_387976.1; NC_000964.3.
DR RefSeq; WP_004399685.1; NZ_JNCM01000029.1.
DR PDB; 4OUN; X-ray; 1.80 A; A=1-143.
DR PDB; 6TNN; EM; 3.07 A; H/I=1-143.
DR PDBsum; 4OUN; -.
DR PDBsum; 6TNN; -.
DR AlphaFoldDB; O31418; -.
DR SMR; O31418; -.
DR STRING; 224308.BSU00950; -.
DR PaxDb; O31418; -.
DR PRIDE; O31418; -.
DR EnsemblBacteria; CAB11871; CAB11871; BSU_00950.
DR GeneID; 936369; -.
DR KEGG; bsu:BSU00950; -.
DR PATRIC; fig|224308.179.peg.98; -.
DR eggNOG; COG1939; Bacteria.
DR InParanoid; O31418; -.
DR OMA; AYMGDAI; -.
DR PhylomeDB; O31418; -.
DR BioCyc; BSUB:BSU00950-MON; -.
DR BRENDA; 3.1.26.3; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR HAMAP; MF_01468; RNase_Mini_III; 1.
DR InterPro; IPR008226; Mini3_fam.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR PIRSF; PIRSF005520; UCP005520; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding.
FT CHAIN 1..143
FT /note="Mini-ribonuclease 3"
FT /id="PRO_0000390306"
FT ACT_SITE 23
FT /evidence="ECO:0000305"
FT MUTAGEN 23
FT /note="D->N: Catalytic mutant, no alteration in rRNA
FT binding."
FT /evidence="ECO:0000269|PubMed:19154332"
FT MUTAGEN 41..43
FT /note="KPN->AAA: Retains nuclease activity, still
FT stimulated by L3."
FT /evidence="ECO:0000269|PubMed:19154332"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4OUN"
FT HELIX 15..36
FT /evidence="ECO:0007829|PDB:4OUN"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:4OUN"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:4OUN"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:4OUN"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:4OUN"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:4OUN"
SQ SEQUENCE 143 AA; 16229 MW; 4340C9F0EFE1545B CRC64;
MLEFDTIKDS KQLNGLALAY IGDAIFEVYV RHHLLKQGFT KPNDLHKKSS RIVSAKSQAE
ILFFLQNQSF FTEEEEAVLK RGRNAKSGTT PKNTDVQTYR YSTAFEALLG YLFLEKKEER
LSQLVAEAIQ FGTSGRKTNE SAT
