RNJ1_BACSU
ID RNJ1_BACSU Reviewed; 555 AA.
AC Q45493;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribonuclease J1 {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=rnjA {ECO:0000255|HAMAP-Rule:MF_01491}; Synonyms=ykqC;
GN OrderedLocusNames=BSU14530;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT 168 chromosome: sequencing of a 27 kb segment and identification of several
RT genes in the area.";
RL Microbiology 142:3033-3037(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION AS AN ENDONUCLEASE, COFACTOR, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=15831787; DOI=10.1093/nar/gki505;
RA Even S., Pellegrini O., Zig L., Labas V., Vinh J., Brechemmier-Baey D.,
RA Putzer H.;
RT "Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with
RT functional homology to E.coli RNase E.";
RL Nucleic Acids Res. 33:2141-2152(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=17005971; DOI=10.1099/mic.0.29152-0;
RA Hunt A., Rawlins J.P., Thomaides H.B., Errington J.;
RT "Functional analysis of 11 putative essential genes in Bacillus subtilis.";
RL Microbiology 152:2895-2907(2006).
RN [6]
RP FUNCTION AS AN EXONUCLEASE, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF HIS-76.
RX PubMed=17512403; DOI=10.1016/j.cell.2007.02.051;
RA Mathy N., Benard L., Pellegrini O., Daou R., Wen T., Condon C.;
RT "5'-to-3' exoribonuclease activity in bacteria: role of RNase J1 in rRNA
RT maturation and 5' stability of mRNA.";
RL Cell 129:681-692(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-76.
RC STRAIN=168;
RX PubMed=17229210; DOI=10.1111/j.1365-2958.2006.05499.x;
RA Britton R.A., Wen T., Schaefer L., Pellegrini O., Uicker W.C., Mathy N.,
RA Tobin C., Daou R., Szyk J., Condon C.;
RT "Maturation of the 5' end of Bacillus subtilis 16S rRNA by the essential
RT ribonuclease YkqC/RNase J1.";
RL Mol. Microbiol. 63:127-138(2007).
RN [8]
RP FUNCTION IN PRE-SCRNA PROCESSING, AND DISRUPTION PHENOTYPE.
RX PubMed=17576666; DOI=10.1093/nar/gkm460;
RA Yao S., Blaustein J.B., Bechhofer D.H.;
RT "Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an
RT additional endonuclease cleavage site.";
RL Nucleic Acids Res. 35:4464-4473(2007).
RN [9]
RP FUNCTION IN MRNA DECAY, AND DISRUPTION PHENOTYPE.
RX PubMed=18445592; DOI=10.1074/jbc.m801461200;
RA Deikus G., Condon C., Bechhofer D.H.;
RT "Role of Bacillus subtilis RNase J1 endonuclease and 5'-exonuclease
RT activities in trp leader RNA turnover.";
RL J. Biol. Chem. 283:17158-17167(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18713320; DOI=10.1111/j.1365-2958.2008.06400.x;
RA Mader U., Zig L., Kretschmer J., Homuth G., Putzer H.;
RT "mRNA processing by RNases J1 and J2 affects Bacillus subtilis gene
RT expression on a global scale.";
RL Mol. Microbiol. 70:183-196(2008).
RN [11]
RP FUNCTION AS AN ENDONUCLEASE, DOMAIN, AND MUTAGENESIS OF ASP-45;
RP 78-ASP-HIS-79; ASN-337 AND SER-366.
RX PubMed=18204464; DOI=10.1038/nsmb.1376;
RA Li de la Sierra-Gallay I., Zig L., Jamalli A., Putzer H.;
RT "Structural insights into the dual activity of RNase J.";
RL Nat. Struct. Mol. Biol. 15:206-212(2008).
RN [12]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=19193632; DOI=10.1074/mcp.m800546-mcp200;
RA Commichau F.M., Rothe F.M., Herzberg C., Wagner E., Hellwig D.,
RA Lehnik-Habrink M., Hammer E., Volker U., Stulke J.;
RT "Novel activities of glycolytic enzymes in Bacillus subtilis: interactions
RT with essential proteins involved in mRNA processing.";
RL Mol. Cell. Proteomics 8:1350-1360(2009).
RN [13]
RP FUNCTION IN 23S RRNA PROCESSING, RNASE ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19880604; DOI=10.1128/jb.01096-09;
RA Redko Y., Condon C.;
RT "Maturation of 23S rRNA in Bacillus subtilis in the absence of Mini-III.";
RL J. Bacteriol. 192:356-359(2010).
RN [14]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH RNASE J2, AND
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=20025672; DOI=10.1111/j.1365-2958.2009.07004.x;
RA Mathy N., Hebert A., Mervelet P., Benard L., Dorleans A.,
RA Li de la Sierra-Gallay I., Noirot P., Putzer H., Condon C.;
RT "Bacillus subtilis ribonucleases J1 and J2 form a complex with altered
RT enzyme behaviour.";
RL Mol. Microbiol. 75:489-498(2010).
RN [15]
RP INTERACTION WITH RNY, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=21803996; DOI=10.1128/jb.05500-11;
RA Lehnik-Habrink M., Newman J., Rothe F.M., Solovyova A.S., Rodrigues C.,
RA Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
RT "RNase Y in Bacillus subtilis: a natively disordered protein that is the
RT functional equivalent of RNase E from Escherichia coli.";
RL J. Bacteriol. 193:5431-5441(2011).
RN [16]
RP FUNCTION.
RX PubMed=22014150; DOI=10.1111/j.1365-2958.2011.07888.x;
RA Taverniti V., Forti F., Ghisotti D., Putzer H.;
RT "Mycobacterium smegmatis RNase J is a 5'-3' exo-/endoribonuclease and both
RT RNase J and RNase E are involved in ribosomal RNA maturation.";
RL Mol. Microbiol. 82:1260-1276(2011).
RN [17]
RP FUNCTION, INTERACTION WITH RNASE J2, AND SUBUNIT.
RX PubMed=21893286; DOI=10.1016/j.str.2011.06.018;
RA Dorleans A., Li de la Sierra-Gallay I., Piton J., Zig L., Gilet L.,
RA Putzer H., Condon C.;
RT "Molecular basis for the recognition and cleavage of RNA by the
RT bifunctional 5'-3' exo/endoribonuclease RNase J.";
RL Structure 19:1252-1261(2011).
RN [18]
RP INTERACTION WITH PNP, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=22198292; DOI=10.1016/j.jmb.2011.12.024;
RA Newman J.A., Hewitt L., Rodrigues C., Solovyova A.S., Harwood C.R.,
RA Lewis R.J.;
RT "Dissection of the network of interactions that links RNA processing with
RT glycolysis in the Bacillus subtilis degradosome.";
RL J. Mol. Biol. 416:121-136(2012).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=22412379; DOI=10.1371/journal.pgen.1002520;
RA Durand S., Gilet L., Bessieres P., Nicolas P., Condon C.;
RT "Three essential ribonucleases-RNase Y, J1, and III-control the abundance
RT of a majority of Bacillus subtilis mRNAs.";
RL PLoS Genet. 8:E1002520-E1002520(2012).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642, 168 / PY79, 168 / W168, and 168 trpC2;
RX PubMed=23504012; DOI=10.1128/jb.00164-13;
RA Figaro S., Durand S., Gilet L., Cayet N., Sachse M., Condon C.;
RT "Bacillus subtilis mutants with knockouts of the genes encoding
RT ribonucleases RNase Y and RNase J1 are viable, with major defects in cell
RT morphology, sporulation, and competence.";
RL J. Bacteriol. 195:2340-2348(2013).
RN [21]
RP INDUCTION.
RC STRAIN=168 / BSB1;
RX PubMed=25092033; DOI=10.1128/jb.02020-14;
RA Keller A.N., Yang X., Wiedermannova J., Delumeau O., Krasny L., Lewis P.J.;
RT "epsilon, a new subunit of RNA polymerase found in gram-positive
RT bacteria.";
RL J. Bacteriol. 196:3622-3632(2014).
RN [22]
RP FUNCTION IN TYPE I TOXIN-ANTITOXIN BSRE/SR5 DEGRADATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / DB104;
RX PubMed=26940229; DOI=10.1080/15476286.2016.1156288;
RA Mueller P., Jahn N., Ring C., Maiwald C., Neubert R., Meissner C.,
RA Brantl S.;
RT "A multistress responsive type I toxin-antitoxin system: bsrE/SR5 from the
RT B. subtilis chromosome.";
RL RNA Biol. 13:511-523(2016).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN OPEN CONFORMATION, ACTIVE SITE,
RP DISCUSSION OF MECHANISM, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=21893285; DOI=10.1016/j.str.2011.06.017;
RA Newman J.A., Hewitt L., Rodrigues C., Solovyova A., Harwood C.R.,
RA Lewis R.J.;
RT "Unusual, dual endo- and exonuclease activity in the degradosome explained
RT by crystal structure analysis of RNase J1.";
RL Structure 19:1241-1251(2011).
CC -!- FUNCTION: An RNase that has endonuclease and 5'-3' exonuclease
CC activity, playing a role in both rRNA and mRNA stability and
CC degradation. Endonuclease activity can cleave within 4 nucleotides of
CC the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the
CC RNase J1/J2 complex occurs at a different site and in some cases more
CC efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2
CC complex is highly processive on substrates longer than 5 nucleotides,
CC on shorter substrates is distributive. Preferentially cleaves ssRNA,
CC possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-
CC hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can
CC digest through stem-loop structures if they are not too stable.
CC Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA
CC precursors after association of the 30S and 50S ribosomal subunits.
CC Plays a role in the secondary pathway of 23S rRNA 5' end maturation.
CC Probably also participates in processing of pre-scRNA (the precursor of
CC the signal recognition particle RNA). Major RNase that degrades both
CC RNAs of the type I toxin-antitoxin system BsrE/SR5 (PubMed:26940229).
CC {ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:17229210,
CC ECO:0000269|PubMed:17512403, ECO:0000269|PubMed:17576666,
CC ECO:0000269|PubMed:18204464, ECO:0000269|PubMed:18445592,
CC ECO:0000269|PubMed:18713320, ECO:0000269|PubMed:19880604,
CC ECO:0000269|PubMed:20025672, ECO:0000269|PubMed:21893286,
CC ECO:0000269|PubMed:22014150, ECO:0000269|PubMed:22412379,
CC ECO:0000269|PubMed:23504012, ECO:0000269|PubMed:26940229}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15831787};
CC Note=Binds 1 Ca(2+) cation per subunit. Seen in 1 crystal structure, it
CC is not clear if it is physiologically important.
CC {ECO:0000269|PubMed:15831787};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15831787};
CC Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
CC Mg(2+) is physiologically important. {ECO:0000269|PubMed:15831787};
CC -!- ACTIVITY REGULATION: 30S ribosomal subunit binding to Shine-Dalgarno
CC sequences blocks exonuclease activity. {ECO:0000269|PubMed:17512403}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 uM for exonuclease on 30 nt RNA hybridized to 17 nt quenching
CC DNA, J1 alone {ECO:0000269|PubMed:20025672};
CC KM=0.22 uM for exonuclease on 30 nt RNA hybridized to 17 nt quenching
CC DNA, J1/J2 complex {ECO:0000269|PubMed:20025672};
CC Note=kcat is 0.58 sec (-1) for J1, 0.13 sec (-1) for J1/J2 and <0.005
CC sec (-1) for J2.;
CC -!- SUBUNIT: Unclear whether it forms homodimers or belongs to a larger
CC complex. According to (PubMed:20025672) probably does not form
CC homodimers, while (PubMed:21893285) shows homodimer formation. Both
CC reports show RNase J1 and J2 interaction, probably as a heterotetramer
CC (PubMed:19193632) shows it is a component of a possible RNA degradosome
CC complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, while
CC (PubMed:20025672) finds no evidence of an RNA degradosome complex.
CC {ECO:0000269|PubMed:19193632, ECO:0000269|PubMed:20025672,
CC ECO:0000269|PubMed:21803996, ECO:0000269|PubMed:21893285,
CC ECO:0000269|PubMed:21893286, ECO:0000269|PubMed:22198292}.
CC -!- INTERACTION:
CC Q45493; Q45493: rnjA; NbExp=5; IntAct=EBI-6415229, EBI-6415229;
CC Q45493; O31760: rnjB; NbExp=4; IntAct=EBI-6415229, EBI-6415198;
CC Q45493; O31774: rny; NbExp=2; IntAct=EBI-6415229, EBI-6415578;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491,
CC ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:17005971}.
CC Note=Colocalizes with ribosomes.
CC -!- INDUCTION: Part of the rpoY-rnjA operon, transcribed constitutively.
CC {ECO:0000269|PubMed:25092033}.
CC -!- DOMAIN: The C-terminal domain (residues 450-555) are required for
CC nuclease activity and dimerization. {ECO:0000269|PubMed:18204464}.
CC -!- DISRUPTION PHENOTYPE: Essential. In depletion experiments there is
CC decreased 5'-exonuclease processing of 16S rRNA (PubMed:17512403),
CC decreased accumulation of correctly-sized scRNA (PubMed:17576666),
CC decreased decay of trp mRNA leader (PubMed:18445592), while correct
CC processing of the 5' end of 23S rRNA no longer occurs in the absence of
CC mrnC (PubMed:19880604). While depletion/deletion of RNase J1 or J2 has
CC no large impact on global gene expression, a double mutant alters the
CC expression of hundreds of genes (PubMed:18713320). In a more severe
CC depletion experiment alteration of about 30% of transcripts was seen
CC (PubMed:22412379). Later shown not to be essential in 4 strains, with a
CC tripled doubling time. 168 trpC2 cells able to grow on minimal medium.
CC Loss of competence for plasmid transformation, nearly complete loss of
CC sporulation, poor growth at 30 degrees Celsius and no growth under 25
CC degrees Celsius. Increased sensitivity to a wide range of antibiotics.
CC Irregularly shaped cells form clumps of spiral cells connected by long
CC chains, with few visible septa, cell walls are altered with looser,
CC less dense peptidoglycan. Double pnp-rnjA or rnjA-rny mutants could not
CC be isolated (PubMed:23504012). Increased half-life of both RNAs of the
CC type I toxin-antitoxin system BsrE/SR5 (PubMed:26940229).
CC {ECO:0000269|PubMed:17005971, ECO:0000269|PubMed:17229210,
CC ECO:0000269|PubMed:17512403, ECO:0000269|PubMed:17576666,
CC ECO:0000269|PubMed:18445592, ECO:0000269|PubMed:18713320,
CC ECO:0000269|PubMed:19880604, ECO:0000269|PubMed:22412379,
CC ECO:0000269|PubMed:23504012, ECO:0000269|PubMed:26940229}.
CC -!- MISCELLANEOUS: Present in about 2500 monomers per cell in mid-log
CC phase.
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; AF012285; AAC24928.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13326.1; -; Genomic_DNA.
DR PIR; B69862; B69862.
DR RefSeq; NP_389336.1; NC_000964.3.
DR RefSeq; WP_003245660.1; NZ_JNCM01000035.1.
DR PDB; 3ZQ4; X-ray; 3.00 A; A/C/D/E=1-555.
DR PDBsum; 3ZQ4; -.
DR AlphaFoldDB; Q45493; -.
DR SMR; Q45493; -.
DR DIP; DIP-46392N; -.
DR IntAct; Q45493; 3.
DR MINT; Q45493; -.
DR STRING; 224308.BSU14530; -.
DR jPOST; Q45493; -.
DR PaxDb; Q45493; -.
DR PRIDE; Q45493; -.
DR EnsemblBacteria; CAB13326; CAB13326; BSU_14530.
DR GeneID; 939483; -.
DR KEGG; bsu:BSU14530; -.
DR PATRIC; fig|224308.179.peg.1583; -.
DR eggNOG; COG0595; Bacteria.
DR InParanoid; Q45493; -.
DR OMA; KNTCVFE; -.
DR PhylomeDB; Q45493; -.
DR BioCyc; BSUB:BSU14530-MON; -.
DR SABIO-RK; Q45493; -.
DR EvolutionaryTrace; Q45493; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
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 3D-structure; Calcium; Cytoplasm; Endonuclease; Exonuclease; Hydrolase;
KW Metal-binding; mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW rRNA processing; Zinc.
FT CHAIN 1..555
FT /note="Ribonuclease J1"
FT /id="PRO_0000215268"
FT REGION 450..555
FT /note="Required for endo- and 5'-exonuclease activity and
FT dimerization"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21893285"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21893285"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
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 BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MUTAGEN 45
FT /note="D->A: Slight decrease in endonuclease and 10-fold
FT decrease in 5'-exonuclease activity; when associated with
FT A-337."
FT /evidence="ECO:0000269|PubMed:18204464"
FT MUTAGEN 76
FT /note="H->A: Loss of endo- and 5'-exonuclease activity."
FT /evidence="ECO:0000269|PubMed:17229210,
FT ECO:0000269|PubMed:17512403"
FT MUTAGEN 78..79
FT /note="DH->KA: Severe loss of endo- and 5'-exonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:18204464"
FT MUTAGEN 337
FT /note="N->A: Slight decrease in endonuclease and 10-fold
FT decrease in 5'-exonuclease activity; when associated with
FT A-45."
FT /evidence="ECO:0000269|PubMed:18204464"
FT MUTAGEN 366
FT /note="S->L: 30% endonuclease and 10% 5'-exonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:18204464"
FT STRAND 8..21
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 143..154
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 393..405
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 480..492
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 500..516
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT HELIX 523..542
FT /evidence="ECO:0007829|PDB:3ZQ4"
FT STRAND 547..554
FT /evidence="ECO:0007829|PDB:3ZQ4"
SQ SEQUENCE 555 AA; 61517 MW; 48091B448B8431C9 CRC64;
MKFVKNDQTA VFALGGLGEI GKNTYAVQFQ DEIVLIDAGI KFPEDELLGI DYVIPDYTYL
VKNEDKIKGL FITHGHEDHI GGIPYLLRQV NIPVYGGKLA IGLLRNKLEE HGLLRQTKLN
IIGEDDIVKF RKTAVSFFRT THSIPDSYGI VVKTPPGNIV HTGDFKFDFT PVGEPANLTK
MAEIGKEGVL CLLSDSTNSE NPEFTMSERR VGESIHDIFR KVDGRIIFAT FASNIHRLQQ
VIEAAVQNGR KVAVFGRSME SAIEIGQTLG YINCPKNTFI EHNEINRMPA NKVTILCTGS
QGEPMAALSR IANGTHRQIS INPGDTVVFS SSPIPGNTIS VSRTINQLYR AGAEVIHGPL
NDIHTSGHGG QEEQKLMLRL IKPKFFMPIH GEYRMQKMHV KLATDCGIPE ENCFIMDNGE
VLALKGDEAS VAGKIPSGSV YIDGSGIGDI GNIVLRDRRI LSEEGLVIVV VSIDMDDFKI
SAGPDLISRG FVYMRESGDL INDAQELISN HLQKVMERKT TQWSEIKNEI TDTLAPFLYE
KTKRRPMILP IIMEV
