ID   RNJ2_STAAW              Reviewed;         557 AA.
AC   Q7A115;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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}; OrderedLocusNames=MW1158;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
CC       endoonuclease activity. Involved in maturation of rRNA and in some
CC       organisms also mRNA maturation and/or decay (By similarity).
CC       {ECO:0000250}.
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   -!- 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; BA000033; BAB95023.1; -; Genomic_DNA.
DR   RefSeq; WP_000052590.1; NC_003923.1.
DR   AlphaFoldDB; Q7A115; -.
DR   SMR; Q7A115; -.
DR   EnsemblBacteria; BAB95023; BAB95023; BAB95023.
DR   KEGG; sam:MW1158; -.
DR   HOGENOM; CLU_008727_3_1_9; -.
DR   OMA; FKMDQFP; -.
DR   Proteomes; UP000000418; 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: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   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   RNA-binding; rRNA processing; Zinc.
FT   CHAIN           1..557
FT                   /note="Ribonuclease J 2"
FT                   /id="PRO_0000286850"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
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_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_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_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"
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