RNC_STRP1
ID RNC_STRP1 Reviewed; 230 AA.
AC P66670; Q490B2; Q9A105;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104};
DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104};
GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; Synonyms=acpA;
GN OrderedLocusNames=SPy_0531, M5005_Spy0438;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP FUNCTION IN CRISPR-MEDIATED PLASMID DEFENSE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=21455174; DOI=10.1038/nature09886;
RA Deltcheva E., Chylinski K., Sharma C.M., Gonzales K., Chao Y.,
RA Pirzada Z.A., Eckert M.R., Vogel J., Charpentier E.;
RT "CRISPR RNA maturation by trans-encoded small RNA and host factor RNase
RT III.";
RL Nature 471:602-607(2011).
RN [4]
RP FUNCTION IN CRRNA AND TRACRRNA MATURATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-51 AND 154-ASN--VAL-230.
RX PubMed=24270795; DOI=10.1093/nar/gkt1074;
RA Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L.,
RA Bzdrenga J., Koonin E.V., Charpentier E.;
RT "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and
RT Cas9 among orthologous type II CRISPR-Cas systems.";
RL Nucleic Acids Res. 42:2577-2590(2014).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC primary rRNA transcript to yield the immediate precursors to the large
CC and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs
CC when they are encoded in the rRNA operon (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat) is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). In this
CC organism endogenous ribonuclease 3 and Cas9 are required for correct
CC coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA).
CC Cas9, crRNA and tracrRNA are required for cleavage of invading DNA
CC (PubMed:21455174, PubMed:24270795). {ECO:0000269|PubMed:21455174,
CC ECO:0000269|PubMed:24270795}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- DISRUPTION PHENOTYPE: Loss of correct coprocessing of pre-crRNA and
CC tracrRNA. Loss of immunity against a plasmid with homology to CRISPR
CC spacer sequences. {ECO:0000269|PubMed:21455174,
CC ECO:0000269|PubMed:24270795}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000255|HAMAP-
CC Rule:MF_00104}.
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DR EMBL; AE004092; AAK33526.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51056.1; -; Genomic_DNA.
DR RefSeq; NP_268805.1; NC_002737.2.
DR AlphaFoldDB; P66670; -.
DR SMR; P66670; -.
DR STRING; 1314.HKU360_00461; -.
DR PaxDb; P66670; -.
DR EnsemblBacteria; AAK33526; AAK33526; SPy_0531.
DR KEGG; spy:SPy_0531; -.
DR KEGG; spz:M5005_Spy0438; -.
DR PATRIC; fig|160490.10.peg.453; -.
DR HOGENOM; CLU_000907_1_3_9; -.
DR OMA; LTHKSCK; -.
DR BRENDA; 3.1.26.3; 11745.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
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; 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; 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 Antiviral defense; Cytoplasm; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1..230
FT /note="Ribonuclease 3"
FT /id="PRO_0000180443"
FT DOMAIN 1..134
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 160..229
FT /note="DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 51
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT MUTAGEN 51
FT /note="D->A: No processing of pre-crRNA."
FT /evidence="ECO:0000269|PubMed:24270795"
FT MUTAGEN 154..230
FT /note="Missing: No processing of pre-crRNA."
FT /evidence="ECO:0000269|PubMed:24270795"
SQ SEQUENCE 230 AA; 25848 MW; 20076A9055B59B4E CRC64;
MKQLEELLST SFDIQFNDLT LLETAFTHTS YANEHRLLNV SHNERLEFLG DAVLQLIISE
YLFAKYPKKT EGDMSKLRSM IVREESLAGF SRFCSFDAYI KLGKGEEKSG GRRRDTILGD
LFEAFLGALL LDKGIDAVRR FLKQVMIPQV EKGNFERVKD YKTCLQEFLQ TKGDVAIDYQ
VISEKGPAHA KQFEVSIVVN GAVLSKGLGK SKKLAEQDAA KNALAQLSEV
