RNJ_HELPY
ID RNJ_HELPY Reviewed; 689 AA.
AC P56185;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=HP_1430;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RHPA, AND SUBUNIT.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=23093592; DOI=10.1093/nar/gks945;
RA Redko Y., Aubert S., Stachowicz A., Lenormand P., Namane A., Darfeuille F.,
RA Thibonnier M., De Reuse H.;
RT "A minimal bacterial RNase J-based degradosome is associated with
RT translating ribosomes.";
RL Nucleic Acids Res. 41:288-301(2013).
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly
CC endoonuclease activity. Involved in maturation of mRNA but apparently
CC not rRNA (By similarity). {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 (Probable). Interacts with RNA helicase RhpA.
CC {ECO:0000269|PubMed:23093592, ECO:0000305}.
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; AE000511; AAD08469.1; -; Genomic_DNA.
DR PIR; F64698; F64698.
DR RefSeq; NP_208221.1; NC_000915.1.
DR RefSeq; WP_000131629.1; NC_018939.1.
DR AlphaFoldDB; P56185; -.
DR SMR; P56185; -.
DR DIP; DIP-3218N; -.
DR IntAct; P56185; 14.
DR MINT; P56185; -.
DR STRING; 85962.C694_07395; -.
DR PaxDb; P56185; -.
DR EnsemblBacteria; AAD08469; AAD08469; HP_1430.
DR KEGG; hpy:HP_1430; -.
DR PATRIC; fig|85962.47.peg.1534; -.
DR eggNOG; COG0595; Bacteria.
DR OMA; KNTCVFE; -.
DR PhylomeDB; P56185; -.
DR Proteomes; UP000000429; 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 InterPro; IPR001587; RNase_J_CS.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 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; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing; Zinc.
FT CHAIN 1..689
FT /note="Ribonuclease J"
FT /id="PRO_0000215269"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206
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 208
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 210
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 211
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 275
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 297
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 297
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 498..502
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491"
FT BINDING 524
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"
SQ SEQUENCE 689 AA; 77386 MW; 77791982943F5B80 CRC64;
MTDNNQNNEN HENSSENSKA DEMRAGAFER FTNRKKRFRE NAQKNAEYSN HEASSHHKKE
HRPNKKPNNH HKQKHAKTRN YAQEELDSNK VEGVTEILHV NERGTLGFHK ELKKGVEANN
KIQVEHLNPH YKMNLNSKAS VKITPLGGLG EIGGNMMVIE TPKSAIVIDA GMSFPKEGLF
GVDILIPDFS YLHQIKDKIA GIIITHAHED HIGATPYLFK ELQFPLYGTP LSLGLIGSKF
DEHGLKKYRS YFKIVEKRCP ISVGEFIIEW IHITHSIIDS SALAIQTKAG TIIHTGDFKI
DHTPVDNLPT DLYRLAHYGE KGVMLLLSDS TNSHKSGTTP SESTIAPAFD TLFKEAQGRV
IMSTFSSNIH RVYQAIQYGI KYNRKIAVIG RSMEKNLDIA RELGYIHLPY QSFIEANEVA
KYPDNEILIV TTGSQGETMS ALYRMATDEH RHISIKPNDL VIISAKAIPG NEASVSAVLN
FLIKKEAKVA YQEFDNIHVS GHAAQEEQKL MLRLIKPKFF LPVHGEYNHV ARHKQTAISC
GVPEKNIYLM EDGDQVEVGP AFIKKVGTIK SGKSYVDNQS NLSIDTSIVQ QREEVASAGV
FVATIFVNKN KQALLESSQF SSLGLVGFKD EKPLIKEIQG GLEVLLKSSN AEILNNPKKL
EDHTRNFIRK ALFKKFRKYP AIICHAHSF
