RNJ_MYCTU
ID RNJ_MYCTU Reviewed; 558 AA.
AC P9WGZ9; L0TAS3; O33294; Q7D6N2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
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};
DE AltName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=Rv2752c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-502, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP FUNCTION AS A BETA-LACTAMASE, FUNCTION AS AN RNASE, ACTIVITY REGULATION,
RP INTERACTION WITH DNAJ2, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-184 AND
RP HIS-397.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21568871; DOI=10.1134/s0006297911030096;
RA Sun L., Zhang L., Zhang H., He Z.G.;
RT "Characterization of a bifunctional beta-lactamase/ribonuclease and its
RT interaction with a chaperone-like protein in the pathogen Mycobacterium
RT tuberculosis H37Rv.";
RL Biochemistry (Mosc.) 76:350-358(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possible endonuclease
CC activity. Involved in maturation of rRNA and in some organisms also
CC mRNA maturation and/or decay (By similarity). Has both beta-lactamase
CC and RNase activity, but the physiological relevance of the beta-
CC lactamase activity, i.e. whether it confers antibiotic resistance, has
CC not been shown (PubMed:21568871). {ECO:0000250,
CC ECO:0000269|PubMed:21568871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
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 -!- ACTIVITY REGULATION: Both beta-lactamase and RNase activities are
CC inhibited by chaperone DnaJ2. {ECO:0000269|PubMed:21568871}.
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome (By
CC similarity). Interacts with chaperone DnaJ2. {ECO:0000255|HAMAP-
CC Rule:MF_01491, ECO:0000269|PubMed:21568871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
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; AL123456; CCP45551.1; -; Genomic_DNA.
DR PIR; G70879; G70879.
DR RefSeq; NP_217268.1; NC_000962.3.
DR RefSeq; WP_003414049.1; NZ_NVQJ01000020.1.
DR AlphaFoldDB; P9WGZ9; -.
DR SMR; P9WGZ9; -.
DR STRING; 83332.Rv2752c; -.
DR PaxDb; P9WGZ9; -.
DR PRIDE; P9WGZ9; -.
DR DNASU; 887802; -.
DR GeneID; 887802; -.
DR KEGG; mtu:Rv2752c; -.
DR TubercuList; Rv2752c; -.
DR eggNOG; COG0595; Bacteria.
DR OMA; KNTCVFE; -.
DR PhylomeDB; P9WGZ9; -.
DR Proteomes; UP000001584; 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:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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: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; 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; Isopeptide bond;
KW Metal-binding; Nuclease; Reference proteome; RNA-binding; rRNA processing;
KW Ubl conjugation; Zinc.
FT CHAIN 1..558
FT /note="Ribonuclease J"
FT /id="PRO_0000395887"
FT REGION 1..269
FT /note="Not absolutely required for RNase activity"
FT REGION 451..558
FT /note="Required for beta-lactamase activity"
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 CROSSLNK 502
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT MUTAGEN 184
FT /note="D->A: Significantly decreased beta-lactamase and
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:21568871"
FT MUTAGEN 397
FT /note="H->V: Significantly decreased beta-lactamase and
FT RNase activity."
FT /evidence="ECO:0000269|PubMed:21568871"
SQ SEQUENCE 558 AA; 59533 MW; D2AFF57234CB4645 CRC64;
MDVDLPPPGP LTSGGLRVTA LGGINEIGRN MTVFEHLGRL LIIDCGVLFP GHDEPGVDLI
LPDMRHVEDR LDDIEALVLT HGHEDHIGAI PFLLKLRPDI PVVGSKFTLA LVAEKCREYR
ITPVFVEVRE GQSTRHGVFE CEYFAVNHST PDALAIAVYT GAGTILHTGD IKFDQLPPDG
RPTDLPGMSR LGDTGVDLLL CDSTNAEIPG VGPSESEVGP TLHRLIRGAD GRVIVACFAS
NVDRVQQIID AAVALGRRVS FVGRSMVRNM RVARQLGFLR VADSDLIDIA AAETMAPDQV
VLITTGTQGE PMSALSRMSR GEHRSITLTA GDLIVLSSSL IPGNEEAVFG VIDALSKIGA
RVVTNAQARV HVSGHAYAGE LLFLYNGVRP RNVMPVHGTW RMLRANAKLA ASTGVPQESI
LLAENGVSVD LVAGKASISG AVPVGKMFVD GLIAGDVGDI TLGERLILSS GFVAVTVVVR
RGTGQPLAAP HLHSRGFSED PKALEPAVRK VEAELESLVA ANVTDPIRIA QGVRRTVGKW
VGETYRRQPM IVPTVIEV
