RNE_BUCAP
ID RNE_BUCAP Reviewed; 968 AA.
AC Q8K9J9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ribonuclease E {ECO:0000255|HAMAP-Rule:MF_00970};
DE Short=RNase E {ECO:0000255|HAMAP-Rule:MF_00970};
DE EC=3.1.26.12 {ECO:0000255|HAMAP-Rule:MF_00970};
GN Name=rne {ECO:0000255|HAMAP-Rule:MF_00970}; OrderedLocusNames=BUsg_335;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00970};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00970};
CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00970};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00970};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00970};
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation. Within the RNA
CC degradosome, RNase E assembles into a homotetramer formed by a dimer of
CC dimers. {ECO:0000255|HAMAP-Rule:MF_00970}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00970}. Cell
CC inner membrane {ECO:0000255|HAMAP-Rule:MF_00970}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00970}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_00970}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00970}.
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DR EMBL; AE013218; AAM67889.1; -; Genomic_DNA.
DR RefSeq; WP_011053856.1; NC_004061.1.
DR AlphaFoldDB; Q8K9J9; -.
DR SMR; Q8K9J9; -.
DR STRING; 198804.BUsg_335; -.
DR EnsemblBacteria; AAM67889; AAM67889; BUsg_335.
DR KEGG; bas:BUsg_335; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_4_6; -.
DR OMA; TQINSAF; -.
DR OrthoDB; 225555at2; -.
DR Proteomes; UP000000416; 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:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 Gene3D; 2.40.50.140; -; 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; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR30001; PTHR30001; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00757; RNaseEG; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytoplasm; Endonuclease; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Nuclease; RNA-binding; rRNA processing;
KW rRNA-binding; tRNA processing; tRNA-binding; Zinc.
FT CHAIN 1..968
FT /note="Ribonuclease E"
FT /id="PRO_0000097371"
FT DOMAIN 39..119
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT REGION 404..407
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT REGION 947..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
SQ SEQUENCE 968 AA; 112656 MW; 460FEF8A218998D0 CRC64;
MKRMLINATQ QEELRVALVD GQRLYDLDIE SSRSEQKKSN IYKGKITRIE PSLEAVFIDY
GMEKHGFLPL KEISKNYFPE NYNCDVRLNI KDILREGQEL IVQINKEERG TKGAALTTFI
TLAGSYLVLM PNNPKIAGIS RRVEGSDRIE LKELLSSLKI PEKMGLIIRT AGVGKSIKSL
QWDLSLRLKH WNAIKKASKK KSAPFLIYQE SNVIVRAFRD YLRQDIGEIL IDNPKILDIA
REHITALGRP DFINKIKLYT GEIPLFSYYQ IESQIDSAFQ RKVRLPSGGS IMVDTTEALT
AIDINSSRST RGADIETTAF NTNLEAVEEI SRQLRLRDLG GLIVIDFIDM TTISHQKIIE
NKLREIVRED RARIQIGHIS KFGLLEMSRQ RLSSSLGESS HHICPRCTGT GTIRDNESLS
LSILRLIEEE ALKENTYEVH AIVPIEIACY LLNEKREAVY AIEKRQAGGK TIIVPNKNMK
TPHYLVSRIR KGEQIRSMSY CLSNVRKNKI FNNIKKEIVD KKHKLNSTLT NISLSDDSFD
KQKEEKEKFL RKKNYNNSII NALFNNKNLF FKFIVWIKNS FLKKHIFVKN ESFKRNIFQN
KKNILFAKKE EFNSIEEIHK KDNQVSSIDN NKKKQLLNKV KKNNNHQYSH VFDNNTKYTS
LKKIDFQKNT IDFELNSLNF LKKNNFYIFS KYNFLYTKKY AKNKFKDFEN IKSQNDMICY
ESFQKDLENN TSFKKKLLYN IIFNNCYPNN ILVNINSTIF QIYKNSEFFK FFPIKISILM
TPLNIFSLEL ILEPSSKKCS SFKENQVKKR LRINNYKKLN SSFIHKKNNF VKNSVLWPKK
FTTEEIKINH LYKKNKKNTK SYFFETSFKY KTVTKNISKL KVKLTSKKND YLISNQKKLF
LNKTLKKENT KNKSSAPITK IFSDVFLSKN QKIMNSSIFL KKSNKKIKNS AGAHSATNFS
TSPVKKSE
