RNJ1_STRP3
ID RNJ1_STRP3 Reviewed; 560 AA.
AC Q8K5W8; Q79YH0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ribonuclease J 1 {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J 1 {ECO:0000255|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN Name=rnj1 {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=SpyM3_1620;
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 J2 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 up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+)
CC or Mg(2+) is physiologically important. {ECO:0000255|HAMAP-
CC 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). Probably a
CC monocistronic operon. {ECO:0000269|PubMed:20025665}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted. Depletion
CC experiments show it is involved in, and may be rate-limiting for decay
CC of Class I mRNAs (they decay rapidly in exponential phase, are
CC difficult to detect in stationary phase). May be required for
CC initiation of decay of Class II mRNAs (more abundant in stationary than
CC exponential phase, show biphasic decay kinetics).
CC {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; AAM80227.1; -; Genomic_DNA.
DR RefSeq; WP_011054984.1; NC_004070.1.
DR AlphaFoldDB; Q8K5W8; -.
DR SMR; Q8K5W8; -.
DR EnsemblBacteria; AAM80227; AAM80227; SpyM3_1620.
DR KEGG; spg:SpyM3_1620; -.
DR HOGENOM; CLU_008727_3_1_9; -.
DR OMA; KNTCVFE; -.
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 InterPro; IPR001587; RNase_J_CS.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR PIRSF; PIRSF004803; RnjA; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR00649; MG423; 1.
DR PROSITE; PS01292; UPF0036; 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..560
FT /note="Ribonuclease J 1"
FT /id="PRO_0000429573"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 366..370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
SQ SEQUENCE 560 AA; 61111 MW; 4523A9B06B099D56 CRC64;
MTNISLKPNE VGVFAIGGLG EIGKNTYGIE YQDEIIIVDA GIKFPEDDLL GIDYVIPDYS
YIVDNLDRVK ALVITHGHED HIGGIPFLLK QANIPIYAGP LALALIRGKL EEHGLWREAT
VYEINHNTEL TFKNMSVTFF KTTHSIPEPV GIVIHTPQGK IICTGDFKFD FTPVGDPADL
QRMAALGEEG VLCLLSDSTN AEIPTFTNSE KVVGQSILKI IEGIHGRIIF ASFASNIYRL
QQAAEAAVKT GRKIAVFGRS MEKAIVNGIE LGYIKVPKGT FIEPSELKNL HASEVLIMCT
GSQGESMAAL ARIANGTHRQ VTLQPGDTVI FSSSPIPGNT TSVNKLINTI QEAGVDVIHG
KVNNIHTSGH GGQQEQKLML SLIKPKYFMP VHGEYRMQKI HAGLAMDIGI PKENIFIMEN
GDVLALTSDS ARIAGHFNAQ DIYVDGNGIG DIGAAVLRDR RDLSEDGVVL AVATVDFNTQ
MILAGPDILS RGFIYMRESG DLIRESQRVL FNAIRIALKN KDASIQSVNG AIVNALRPFL
YEKTEREPII IPMVLTPDKH
