RNJ2_STRP3
ID RNJ2_STRP3 Reviewed; 553 AA.
AC Q8K7S6; Q79WZ3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ribonuclease J 2 {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J 2 {ECO:0000255|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN Name=rnj2 {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=SpyM3_0657;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
RN [2]
RP FUNCTION, INDUCTION, OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=20025665; DOI=10.1111/j.1365-2958.2009.07012.x;
RA Bugrysheva J.V., Scott J.R.;
RT "The ribonucleases J1 and J2 are essential for growth and have independent
RT roles in mRNA decay in Streptococcus pyogenes.";
RL Mol. Microbiol. 75:731-743(2010).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC activity. Involved in maturation of rRNA and in some organisms also
CC mRNA maturation and/or decay (By similarity). Has an overlapping but
CC not completely redundant role with RNase J1 in the decay of mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01491, ECO:0000269|PubMed:20025665}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01491};
CC Note=Binds 1 Zn(2+) ion per subunit. It is not clear if Zn(2+) or
CC Mg(2+) is physiologically important. {ECO:0000255|HAMAP-Rule:MF_01491};
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- INDUCTION: Expressed in cells (at protein level). Part of an operon
CC including SpyM3_0658 and probably SpyM3_0659.
CC {ECO:0000269|PubMed:20025665}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted. Depletion
CC experiments show is involved in decay of Class I mRNAs (they decay
CC rapidly in exponential phase, are difficult to detect in stationary
CC phase). Involved in an early stage of degradation of Class II mRNAs
CC (more abundant in stationary than exponential phase, show biphasic
CC decay kinetics). {ECO:0000269|PubMed:20025665}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01491}.
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DR EMBL; AE014074; AAM79264.1; -; Genomic_DNA.
DR RefSeq; WP_002984872.1; NC_004070.1.
DR AlphaFoldDB; Q8K7S6; -.
DR SMR; Q8K7S6; -.
DR EnsemblBacteria; AAM79264; AAM79264; SpyM3_0657.
DR KEGG; spg:SpyM3_0657; -.
DR HOGENOM; CLU_008727_3_1_9; -.
DR OMA; FKMDQFP; -.
DR BRENDA; 4.6.1.22; 5935.
DR Proteomes; UP000000564; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10710; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01491; RNase_J_bact; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR004613; RNase_J.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00649; MG423; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Exonuclease; Hydrolase; Metal-binding;
KW mRNA processing; Nuclease; RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..553
FT /note="Ribonuclease J 2"
FT /id="PRO_0000429574"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 361..365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
SQ SEQUENCE 553 AA; 61179 MW; B1A3F4EA37417603 CRC64;
MTDIKMIALG GVREYGKNFY LVEINDSMFI LDAGLKYPEN EQLGVDLVIP NLDYVIENKG
KVQGIFLSHG HADAIGALPY LLAEVSAPVF GSELTIELAK LFVKSNNSTK KFNNFHVVDS
DTEIEFKDGL VSFFRTTHSI PESMGIVIGT DKGNIVYTGD FKFDQAAREG YQTDLLRLAE
IGKEGVLALL SDSVNATSND QIASESEVGE EMDSVISDAD GRVIVAAVAS NLVRIQQVFD
SATAHGRRVV LTGTDAENIV RTALRLEKLM ITDERLLIKP KDMSKFEDHE LIILEAGRMG
EPINSLQKMA AGRHRYVQIK EGDLVYIVTT PSTAKEAMVA RVENLIYKAG GSVKLITQNL
RVSGHANGRD LQLLMNLLKP QYLFPVQGEY RDLAAHAKLA EEVGIFPENI HILKRGDIMV
LNDEGFLHEG GVPASDVMID GNAIGDVGNI VLRDRKVLSE DGIFIVAITV SKKEKRIISK
AKVNTRGFVY VKKSHDILRE SAELVNTTVG NYLKKDTFDW GELKGNVRDD LSKFLFEQTK
RRPAILPVVM EVR
