RNJ2_STAA8
ID RNJ2_STAA8 Reviewed; 557 AA.
AC Q2FZ19;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ribonuclease J 2 {ECO:0000255|HAMAP-Rule:MF_01491};
DE Short=RNase J2 {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};
GN OrderedLocusNames=SAOUHSC_01252;
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 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 MATURATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 76-HIS--HIS-78.
RC STRAIN=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 probably plays a structural rather than enzymatic role as
CC mutation of its putative active site gives no phenotype, and its
CC deletion is partially complemented by inactive RNase J1.
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 RNase J1. {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, poor growth
CC at 30 degrees Celsius. No growth on other media at 37 degrees Celsius
CC unless supplemented with MgCl(2), nor at 42 or 25 degrees Celsius.
CC Double rnj1-rnj2 mutant grows much slower than either single mutant and
CC only at 37 degrees Celsius. {ECO:0000269|PubMed:22447609,
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD30353.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000253; ABD30353.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000052590.1; NZ_LS483365.1.
DR RefSeq; YP_499785.1; NC_007795.1.
DR AlphaFoldDB; Q2FZ19; -.
DR SMR; Q2FZ19; -.
DR STRING; 1280.SAXN108_1279; -.
DR ABCD; Q2FZ19; 1 sequenced antibody.
DR EnsemblBacteria; ABD30353; ABD30353; SAOUHSC_01252.
DR GeneID; 3919983; -.
DR KEGG; sao:SAOUHSC_01252; -.
DR PATRIC; fig|93061.5.peg.1146; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_1_9; -.
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 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.
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..557
FT /note="Ribonuclease J 2"
FT /id="PRO_0000286837"
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 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 366..370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT MUTAGEN 76..78
FT /note="HGH->AGA: Grows like wild-type."
FT /evidence="ECO:0000269|PubMed:24586213"
SQ SEQUENCE 557 AA; 62604 MW; 7E23A4311DFECBE3 CRC64;
MSLIKKKNKD IRIIPLGGVG EIAKNMYIVE VDDEMFMLDA GLMFPEDEML GIDIVIPDIS
YVLENKDKLK GIFLTHGHEH AIGAVSYVLE QLDAPVYGSK LTIALIKENM KARNIDKKVR
YYTVNNDSIM RFKNVNISFF NTTHSIPDSL GVCIHTSYGA IVYTGEFKFD QSLHGHYAPD
IKRMAEIGEE GVFVLISDST EAEKPGYNTP ENVIEHHMYD AFAKVRGRLI VSCYASNFIR
IQQVLNIASK LNRKVSFLGR SLESSFNIAR KMGYFDIPKD LLIPITEVDN YPKNEVIIIA
TGMQGEPVEA LSQMAQHKHK IMNIEEGDSV FLAITASANM EVIIANTLNE LVRAGAHIIP
NNKKIHASSH GCMEELKMMI NIMKPEYFIP VQGEFKMQIA HAKLAAEAGV APEKIFLVEK
GDVINYNGKD MILNEKVNSG NILIDGIGIG DVGNIVLRDR HLLAEDGIFI AVVTLDPKNR
RIAAGPEIQS RGFVYVRESE DLLREAEEKV REIVEAGLQE KRIEWSEIKQ NMRDQISKLL
FESTKRRPMI IPVISEI
