ID E6YHT3_BARC7 Unreviewed; 804 AA. AC E6YHT3; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 02-SEP-2026, entry version 79. DE RecName: Full=Ribonuclease E {ECO:0000256|HAMAP-Rule:MF_00970}; DE Short=RNase E {ECO:0000256|HAMAP-Rule:MF_00970}; DE EC=3.1.26.12 {ECO:0000256|HAMAP-Rule:MF_00970}; GN Name=rne {ECO:0000256|HAMAP-Rule:MF_00970, GN ECO:0000313|EMBL:CBI76421.1}; GN OrderedLocusNames=BARCL_0740 {ECO:0000313|EMBL:CBI76421.1}; OS Bartonella clarridgeiae (strain CCUG 45776 / CIP 104772 / 73). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Bartonellaceae; Bartonella. OX NCBI_TaxID=696125 {ECO:0000313|EMBL:CBI76421.1, ECO:0000313|Proteomes:UP000009101}; RN [1] {ECO:0000313|Proteomes:UP000009101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101}; RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., Christa L., RA Alexandra C., Aurelie L., Claudine M., Stephan S.C., Christoph D.; RT "Genome sequencing of Bartonella species and comparative genomics."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBI76421.1, ECO:0000313|Proteomes:UP000009101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101}; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating lineages of RT the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA processing CC and decay. Required for the maturation of 5S and 16S rRNAs and the CC majority of tRNAs. Also involved in the degradation of most mRNAs. CC {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U- CC rich regions.; EC=3.1.26.12; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00970}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00970}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00970}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00970}; CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP- CC Rule:MF_00970}; CC -!- SUBUNIT: Homotetramer formed by a dimer of dimers. {ECO:0000256|HAMAP- CC Rule:MF_00970}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}. Cell CC inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral membrane CC protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic side CC {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00970}. 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; FN645454; CBI76421.1; -; Genomic_DNA. DR RefSeq; WP_013545060.1; NC_014932.1. DR AlphaFoldDB; E6YHT3; -. DR STRING; 696125.BARCL_0740; -. DR KEGG; bcd:BARCL_0740; -. DR eggNOG; COG1530; Bacteria. DR HOGENOM; CLU_003468_5_0_5; -. DR Proteomes; UP000009101; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008995; F:ribonuclease E activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. DR CDD; cd04453; S1_RNase_E; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1. DR HAMAP; MF_00970; RNase_E; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G. DR InterPro; IPR028878; RNase_E. DR InterPro; IPR004659; RNase_E/G. DR InterPro; IPR048583; RNase_E_G_thioredoxin-like. DR NCBIfam; TIGR00757; RNaseEG; 1. DR PANTHER; PTHR30001; RIBONUCLEASE; 1. DR PANTHER; PTHR30001:SF1; RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC; 1. DR Pfam; PF10150; RNase_E_G; 1. DR Pfam; PF20833; RNase_E_G_Thio; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00970}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00970}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00970}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00970}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00970}; KW Reference proteome {ECO:0000313|Proteomes:UP000009101}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00970}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00970}. FT DOMAIN 213..483 FT /note="RNA-binding protein AU-1/Ribonuclease E/G" FT /evidence="ECO:0000259|Pfam:PF10150" FT DOMAIN 495..579 FT /note="RNase E/G thioredoxin-like" FT /evidence="ECO:0000259|Pfam:PF20833" FT REGION 496..499 FT /note="Required for zinc-mediated homotetramerization and FT catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT REGION 600..671 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 600..615 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 637..650 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 651..662 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 395 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT BINDING 438 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT BINDING 496 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT BINDING 499 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" SQ SEQUENCE 804 AA; 91737 MW; 611F35D9F7157572 CRC64; MSNKMLIDAS HPEETRVVVV HDNKIEELDF ESEHKKQLKG NIYLARITRI EPSLQAAFVE YGGNRHGFLT FAEIHPDYYQ IPVADRLALL EEEKAVINES YGDDPIEETI QNKKSLRKTK KDKSNSFMAT DIENDIISET IIADDAEEIP DFSNDDIEMV GAEDALEELP TYRRKQGCQY KIQEVIKRRQ ILLIQVIKEE RGNKGAALTT YLSLAGRYSV LMPNTARGGG ISRKITNIQD RKRLKEIVKE LAVPKGMGVI LRTAGANRTK AEIKRDYEYL MRLWDTIRAL TLKSTAPCLI HEESNLIKRS IRDLYSKDIN EILVAGDQGY REAKDFMRML MPSHAKVVQP YRNPIPIFAH NDIETQLDKM LHPQVSLKSG GYLVINQTEA LVAIDVNSGR STKEHSVEKT ALQTNLEAAE EIARQLRLRD LAGLIVIDFI DMLETRNIKL VEKKLKDCLK NDRARIQVGH ISHFGLMEMS RQRIRVSVLE STTQPCPHCA GTGNIRSESS IALHVMRSIE EYLLRNSQYN IIVRTSVATA LYVLNHKRNI LVNLETRFGL SINIEADDSI GTQHLAISKG SIAKGNSFTS TVIEDNDKNT VLMTSKTTKD TTSVENNKRR RRKNNKIESN NDGILADAHK DNTQNDDDTR RRGRRRGRRG GRRNQDNNYQ FRVPYAEPIG DFAKQALEEI KAEYRQYYNI PAAEPVGFNK GTRGYKRHLI STQQDEIIKT HVAIKSTKHN VKSSEPLKNK RSLVKDKNIT TPKQEEFVEE KLVTKSNRKP KIKAINEFAN EVNEEISINK KNQR //