RNJ1_STAA8
ID RNJ1_STAA8 Reviewed; 565 AA.
AC Q2FZG9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ribonuclease J 1 {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J1 {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};
GN OrderedLocusNames=SAOUHSC_01035;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP INTERACTION WITH PNPA AND RNJB, AND SUBUNIT.
RC STRAIN=UAMS-1;
RX PubMed=21764917; DOI=10.1128/jb.05485-11;
RA Roux C.M., DeMuth J.P., Dunman P.M.;
RT "Characterization of components of the Staphylococcus aureus mRNA
RT degradosome holoenzyme-like complex.";
RL J. Bacteriol. 193:5520-5526(2011).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=SA564;
RX PubMed=22447609; DOI=10.1128/aem.00202-12;
RA Redder P., Linder P.;
RT "New range of vectors with a stringent 5-fluoroorotic acid-based
RT counterselection system for generating mutants by allelic replacement in
RT Staphylococcus aureus.";
RL Appl. Environ. Microbiol. 78:3846-3854(2012).
RN [4]
RP FUNCTION IN 16S RRNA; RNPB AND MRNA PROCESSING, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 74-HIS--HIS-76.
RC STRAIN=RN4220, and SA564;
RX PubMed=24586213; DOI=10.1371/journal.pgen.1004207;
RA Linder P., Lemeille S., Redder P.;
RT "Transcriptome-wide analyses of 5'-ends in RNase J mutants of a gram-
RT positive pathogen reveal a role in RNA maturation, regulation and
RT degradation.";
RL PLoS Genet. 10:E1004207-E1004207(2014).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and endonuclease
CC activity, with the exonuclease activity probably being most important
CC in vivo. Involved in maturation of 16S rRNA, rnpB (the RNA component of
CC RNase P) maturation and degradation, and mRNA maturation and/or decay.
CC This subunit has the exonuclease activity.
CC {ECO:0000269|PubMed:24586213}.
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 (By similarity). Component of a possible RNA
CC degradosome complex composed of cshA, eno, pfkA, pnp, rnjA, rnjB, rnpA
CC and rny. Interacts specifically with PNPase and RNase J2. {ECO:0000250,
CC ECO:0000269|PubMed:21764917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
CC -!- DISRUPTION PHENOTYPE: Very sensitive to temperature and medium changes;
CC slow growth at 37 degrees Celsius on Mueller-Hinton medium for clinical
CC strain SA564 or lab strain RN4220. No growth of SA564 grown on other
CC media or at 42, 30 or 25 degrees Celsius. Double rnj1-rnj2 mutant grows
CC much slower than either single mutant and only at 37 degrees Celsius.
CC {ECO:0000269|PubMed:22447609, ECO:0000269|PubMed:24586213}.
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; CP000253; ABD30155.1; -; Genomic_DNA.
DR RefSeq; WP_000811375.1; NZ_LS483365.1.
DR RefSeq; YP_499584.1; NC_007795.1.
DR AlphaFoldDB; Q2FZG9; -.
DR SMR; Q2FZG9; -.
DR STRING; 1280.SAXN108_1085; -.
DR EnsemblBacteria; ABD30155; ABD30155; SAOUHSC_01035.
DR GeneID; 3919883; -.
DR KEGG; sao:SAOUHSC_01035; -.
DR PATRIC; fig|93061.5.peg.951; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_1_9; -.
DR OMA; KNTCVFE; -.
DR Proteomes; UP000008816; 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; Reference proteome; RNA-binding;
KW rRNA processing; Zinc.
FT CHAIN 1..565
FT /note="Ribonuclease J 1"
FT /id="PRO_0000286836"
FT BINDING 74
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 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="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 79
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 142
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 164
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 164
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 364..368
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 390
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 74..76
FT /note="HGH->AGA: Acts like deletion mutant in growth and
FT RNA processing experiments."
FT /evidence="ECO:0000269|PubMed:24586213"
SQ SEQUENCE 565 AA; 62669 MW; B1C619591C2E42B9 CRC64;
MKQLHPNEVG VYALGGLGEI GKNTYAVEYK DEIVIIDAGI KFPDDNLLGI DYVIPDYTYL
VQNQDKIVGL FITHGHEDHI GGVPFLLKQL NIPIYGGPLA LGLIRNKLEE HHLLRTAKLN
EINEDSVIKS KHFTISFYLT THSIPETYGV IVDTPEGKVV HTGDFKFDFT PVGKPANIAK
MAQLGEEGVL CLLSDSTNSL VPDFTLSERE VGQNVDKIFR NCKGRIIFAT FASNIYRVQQ
AVEAAIKNNR KIVTFGRSME NNIKIGMELG YIKAPPETFI EPNKINTVPK HELLILCTGS
QGEPMAALSR IANGTHKQIK IIPEDTVVFS SSPIPGNTKS INRTINSLYK AGADVIHSKI
SNIHTSGHGS QGDQQLMLRL IKPKYFLPIH GEYRMLKAHG ETGVECGVEE DNVFIFDIGD
VLALTHDSAR KAGRIPSGNV LVDGSGIGDI GNVVIRDRKL LSEEGLVIVV VSIDFNTNKL
LSGPDIISRG FVYMRESGQL IYDAQRKIKT DVISKLNQNK DIQWHQIKSS IIETLQPYLF
EKTARKPMIL PVIMKVNEQK ESNNK
