RNJ_MYCS2
ID RNJ_MYCS2 Reviewed; 558 AA.
AC A0QVT2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491};
GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491};
GN OrderedLocusNames=MSMEG_2685, MSMEI_2620;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS AN EXO- AND ENDORIBONUCLEASE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 85-ASP-HIS-86.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=22014150; DOI=10.1111/j.1365-2958.2011.07888.x;
RA Taverniti V., Forti F., Ghisotti D., Putzer H.;
RT "Mycobacterium smegmatis RNase J is a 5'-3' exo-/endoribonuclease and both
RT RNase J and RNase E are involved in ribosomal RNA maturation.";
RL Mol. Microbiol. 82:1260-1276(2011).
CC -!- FUNCTION: An RNase that has endonuclease and 5'-3' exonuclease
CC activity. The 5'-exonuclease activity acts on 5'-monophosphate but not
CC 5'-triphosphate ends. Endonuclease activity can cleave within 4
CC nucleotides of the 5'-end of a triphosphorylated RNA. Plays the major
CC role in pre-23S rRNA maturation, and a minor role in processing of pre-
CC 5S and pre-16S rRNA. {ECO:0000269|PubMed:22014150}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- DISRUPTION PHENOTYPE: Non-essential, it can be deleted. No effect on
CC processing of furA-katG operon mRNA or of pre-5S rRNA processing.
CC Complete loss of mature 23S rRNA. Minor effects on pre-16S rRNA
CC processing. A double rnj-rne depletion mutant indicates this enzyme
CC plays a role in degradation of previously processed pre-16S rRNAs and a
CC decrease in mature 5S rRNA. {ECO:0000269|PubMed:22014150}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK74200.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39088.1; -; Genomic_DNA.
DR RefSeq; WP_003894070.1; NZ_SIJM01000059.1.
DR RefSeq; YP_887020.1; NC_008596.1.
DR AlphaFoldDB; A0QVT2; -.
DR SMR; A0QVT2; -.
DR STRING; 246196.MSMEI_2620; -.
DR EnsemblBacteria; ABK74200; ABK74200; MSMEG_2685.
DR EnsemblBacteria; AFP39088; AFP39088; MSMEI_2620.
DR GeneID; 66734093; -.
DR KEGG; msg:MSMEI_2620; -.
DR KEGG; msm:MSMEG_2685; -.
DR PATRIC; fig|246196.19.peg.2652; -.
DR eggNOG; COG0595; Bacteria.
DR OMA; KNTCVFE; -.
DR OrthoDB; 580619at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
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; PF12706; Lactamase_B_2; 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.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..558
FT /note="Ribonuclease J"
FT /id="PRO_0000429578"
FT BINDING 81
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 83
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 85
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 86
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 148
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 170
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 170
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 371..375
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 397
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 MUTAGEN 85..86
FT /note="DH->KA: Severely decreases 5'-3' exonuclease
FT activity, retains considerable endonuclease activity."
FT /evidence="ECO:0000269|PubMed:22014150"
SQ SEQUENCE 558 AA; 59617 MW; DE2BF91DEFD4AFF8 CRC64;
MSAELAPPPP LAPGGLRVTA LGGISEIGRN MTVFEHLGRL LIVDCGVLFP GHDEPGVDLI
LPDLRHIEDR LDEIEALVVT HAHEDHIGAI PFLLKLRPDI PVVGSKFTIA LVREKCREHR
LKPKFVEVAE RQSSQHGVFE CEYFAVNHSI PGCLAVAIHT GAGTVLHTGD IKLDQLPLDG
RPTDLPGMSR LGDAGVDLFL CDSTNSEHPG VSPSESEVGP TLHRLIRGAE GRVIVACFAS
NVDRVQQIID AAVALGRRVS FVGRSMVRNM GIARELGYLK VDDSDILDIA AAEMMPPDRV
VLITTGTQGE PMAALSRMSR GEHRSITLTS GDLIILSSSL IPGNEEAVYG VIDSLSKIGA
RVVTNAQARV HVSGHAYAGE LLFLYNGVRP RNVMPVHGTW RHLRANAALA ASTGVPPENI
VLAENGVSVD LVAGRASISG AVTVGKMFVD GLITGDVGDA TLGERLILSS GFVSITVVVH
RGTGRPAGPA HLISRGFSED PKALEPVAQK VERELEALAA DNVTDPTRIA QAVRRTVGKW
VGETYRRQPM IVPTVIEI
