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Mini-ribonuclease 3 (Mini-3) (Mini-RNase 3) (EC 3.1.26.-) (Mini-RNase III) (Mini-III)

 MRNC_BACSU              Reviewed;         143 AA.
O31418;
15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 94.
RecName: Full=Mini-ribonuclease 3;
Short=Mini-3;
Short=Mini-RNase 3;
EC=3.1.26.-;
AltName: Full=Mini-RNase III;
Short=Mini-III;
Name=mrnC; Synonyms=yazC; OrderedLocusNames=BSU00950;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[2]
DISCUSSION OF POSSIBLE FUNCTION.
PubMed=16014871; DOI=10.1093/molbev/msi211;
Fang G., Rocha E., Danchin A.;
"How essential are nonessential genes?";
Mol. Biol. Evol. 22:2147-2156(2005).
[3]
FUNCTION IN 23S RRNA PROCESSING, RNASE ACTIVITY, SUBUNIT, COFACTOR,
AND DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=18363798; DOI=10.1111/j.1365-2958.2008.06207.x;
Redko Y., Bechhofer D.H., Condon C.;
"Mini-III, an unusual member of the RNase III family of enzymes,
catalyses 23S ribosomal RNA maturation in B. subtilis.";
Mol. Microbiol. 68:1096-1106(2008).
[4]
STIMULATION BY RPLC (RIBOSOMAL PROTEIN L3), AND MUTAGENESIS OF ASP-23
AND 41-ARG--ASN-43.
PubMed=19154332; DOI=10.1111/j.1365-2958.2008.06591.x;
Redko Y., Condon C.;
"Ribosomal protein L3 bound to 23S precursor rRNA stimulates its
maturation by Mini-III ribonuclease.";
Mol. Microbiol. 71:1145-1154(2009).
-!- FUNCTION: Involved in correct processing of both the 5' and 3'
ends of 23S rRNA precursor. Processes 30S rRNA precursor
transcript even in absence of ribonuclease 3 (Rnc); Rnc processes
30S rRNA into smaller rRNA precursors. Cleaves more efficiently on
assembled 50S ribosomal subunits. Cleavage is strongly stimulated
by ribosomal protein L3 (RplC); 20-30% DMSO can replace RplC,
suggesting RplC may alter rRNA conformation.
{ECO:0000269|PubMed:18363798}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:18363798};
-!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:18363798}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Cells accumulate precursors and mature forms
of 23S rRNA with alternative 5' and 3' ends. Defects are more
marked during exponential growth. {ECO:0000269|PubMed:18363798}.
-!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000305}.
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EMBL; AL009126; CAB11871.1; -; Genomic_DNA.
PIR; C69742; C69742.
RefSeq; NP_387976.1; NC_000964.3.
RefSeq; WP_004399685.1; NZ_JNCM01000029.1.
PDB; 4OUN; X-ray; 1.80 A; A=1-143.
PDBsum; 4OUN; -.
ProteinModelPortal; O31418; -.
SMR; O31418; -.
STRING; 224308.Bsubs1_010100000495; -.
PaxDb; O31418; -.
EnsemblBacteria; CAB11871; CAB11871; BSU00950.
GeneID; 936369; -.
KEGG; bsu:BSU00950; -.
PATRIC; fig|224308.179.peg.98; -.
eggNOG; ENOG4105KEB; Bacteria.
eggNOG; COG1939; LUCA.
HOGENOM; HOG000218681; -.
InParanoid; O31418; -.
KO; K11145; -.
OMA; AIFEVYV; -.
PhylomeDB; O31418; -.
BioCyc; BSUB:BSU00950-MONOMER; -.
BRENDA; 3.1.26.3; 658.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
CDD; cd00593; RIBOc; 1.
Gene3D; 1.10.1520.10; -; 1.
HAMAP; MF_01468; RNase_Mini_III; 1.
InterPro; IPR008226; Mini3_fam.
InterPro; IPR000999; RNase_III_dom.
InterPro; IPR036389; RNase_III_sf.
Pfam; PF00636; Ribonuclease_3; 1.
PIRSF; PIRSF005520; UCP005520; 1.
SMART; SM00535; RIBOc; 1.
SUPFAM; SSF69065; SSF69065; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endonuclease; Hydrolase;
Magnesium; Nuclease; Reference proteome; Ribosome biogenesis;
RNA-binding; rRNA processing; rRNA-binding.
CHAIN 1 143 Mini-ribonuclease 3.
/FTId=PRO_0000390306.
ACT_SITE 23 23 {ECO:0000305}.
MUTAGEN 23 23 D->N: Catalytic mutant, no alteration in
rRNA binding.
{ECO:0000269|PubMed:19154332}.
MUTAGEN 41 43 KPN->AAA: Retains nuclease activity,
still stimulated by L3.
{ECO:0000269|PubMed:19154332}.
HELIX 10 12 {ECO:0000244|PDB:4OUN}.
HELIX 15 36 {ECO:0000244|PDB:4OUN}.
HELIX 42 53 {ECO:0000244|PDB:4OUN}.
HELIX 55 67 {ECO:0000244|PDB:4OUN}.
HELIX 73 83 {ECO:0000244|PDB:4OUN}.
HELIX 96 114 {ECO:0000244|PDB:4OUN}.
HELIX 118 133 {ECO:0000244|PDB:4OUN}.
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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