(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 99.
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}.
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   PDBsum; 4OUN; -.
DR   SMR; O31418; -.
DR   STRING; 224308.BSU00950; -.
DR   PaxDb; O31418; -.
DR   PRIDE; O31418; -.
DR   EnsemblBacteria; CAB11871; CAB11871; BSU00950.
DR   GeneID; 936369; -.
DR   KEGG; bsu:BSU00950; -.
DR   PATRIC; fig|224308.179.peg.98; -.
DR   eggNOG; ENOG4105KEB; Bacteria.
DR   eggNOG; COG1939; LUCA.
DR   HOGENOM; HOG000218681; -.
DR   InParanoid; O31418; -.
DR   KO; K11145; -.
DR   OMA; AIFEVYV; -.
DR   PhylomeDB; O31418; -.
DR   BioCyc; BSUB:BSU00950-MONOMER; -.
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;
DR   PRODOM; O31418.
DR   SWISS-2DPAGE; O31418.
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:0000244|PDB:4OUN"
FT   HELIX           15..36
FT                   /evidence="ECO:0000244|PDB:4OUN"
FT   HELIX           42..53
FT                   /evidence="ECO:0000244|PDB:4OUN"
FT   HELIX           55..67
FT                   /evidence="ECO:0000244|PDB:4OUN"
FT   HELIX           73..83
FT                   /evidence="ECO:0000244|PDB:4OUN"
FT   HELIX           96..114
FT                   /evidence="ECO:0000244|PDB:4OUN"
FT   HELIX           118..133
FT                   /evidence="ECO:0000244|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
//

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