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 27-MAR-2024, entry version 122. 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; Campylobacterota; 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7PCR; X-ray; 2.75 A; A=137-689. DR PDBsum; 7PCR; -. DR AlphaFoldDB; P56185; -. DR SMR; P56185; -. DR DIP; DIP-3218N; -. DR IntAct; P56185; 14. DR MINT; P56185; -. DR STRING; 85962.HP_1430; -. DR PaxDb; 85962-C694_07395; -. DR EnsemblBacteria; AAD08469; AAD08469; HP_1430. DR KEGG; hpy:HP_1430; -. DR PATRIC; fig|85962.47.peg.1534; -. DR eggNOG; COG0595; Bacteria. DR InParanoid; P56185; -. DR OrthoDB; 9770211at2; -. DR PhylomeDB; P56185; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule. DR CDD; cd07714; RNaseJ_MBL-fold; 1. DR Gene3D; 3.10.20.580; -; 1. DR Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1. DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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 NCBIfam; TIGR00649; MG423; 1. DR PANTHER; PTHR43694; RIBONUCLEASE J; 1. DR PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1. 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; Metallo-hydrolase/oxidoreductase; 1. DR PROSITE; PS01292; UPF0036; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Endonuclease; Exonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; RNA-binding; rRNA processing; KW 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" FT STRAND 141..153 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 190..194 FT /evidence="ECO:0007829|PDB:7PCR" FT TURN 195..198 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 215..219 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 230..242 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 246..251 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 266..272 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 280..287 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 312..321 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:7PCR" FT TURN 331..334 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 346..354 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 369..381 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 385..389 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 391..402 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 410..412 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 416..421 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 424..426 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 427..431 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 439..446 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 460..463 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 472..484 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 492..494 FT /evidence="ECO:0007829|PDB:7PCR" FT TURN 496..498 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 505..515 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 517..525 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 527..539 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 544..546 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 554..559 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 562..568 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 573..576 FT /evidence="ECO:0007829|PDB:7PCR" FT TURN 578..580 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 583..585 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 586..596 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 600..607 FT /evidence="ECO:0007829|PDB:7PCR" FT TURN 609..611 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 613..626 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 628..647 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 651..655 FT /evidence="ECO:0007829|PDB:7PCR" FT HELIX 657..676 FT /evidence="ECO:0007829|PDB:7PCR" FT STRAND 681..687 FT /evidence="ECO:0007829|PDB:7PCR" 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 //