RNE_MYCS2
ID RNE_MYCS2 Reviewed; 1037 AA.
AC A0R152;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ribonuclease E;
DE Short=RNase E;
DE EC=3.1.26.12;
GN Name=rne; OrderedLocusNames=MSMEG_4626, MSMEI_4509;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
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).
CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA processing
CC and decay. Plays a major role in pre-16S rRNA maturation, probably
CC generating the mature 5'-end, and a minor role in pre-5S and pre-23S
CC rRNA maturation (PubMed:22014150). Probably also processes tRNA (By
CC similarity). {ECO:0000250|UniProtKB:P21513,
CC ECO:0000269|PubMed:22014150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-
CC rich regions.; EC=3.1.26.12;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 2 Zn(2+) ions per homotetramer. Zinc ions are bound between
CC subunits. {ECO:0000250|UniProtKB:P21513};
CC -!- SUBUNIT: Assembles into a homotetramer formed by a dimer of dimers.
CC {ECO:0000250|UniProtKB:P21513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21513}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. Depletion
CC experiments show decreased processing of furA-katG operon mRNA, altered
CC processing of pre-16S rRNA, minor effects on pre-23S rRNA processing. A
CC double rnj-rne depletion mutant has decreased amounts of mature 5S
CC rRNA. {ECO:0000269|PubMed:22014150}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. {ECO:0000305}.
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DR EMBL; CP000480; ABK75182.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40963.1; -; Genomic_DNA.
DR RefSeq; WP_011729971.1; NZ_SIJM01000004.1.
DR RefSeq; YP_888890.1; NC_008596.1.
DR AlphaFoldDB; A0R152; -.
DR SMR; A0R152; -.
DR STRING; 246196.MSMEI_4509; -.
DR PRIDE; A0R152; -.
DR EnsemblBacteria; ABK75182; ABK75182; MSMEG_4626.
DR EnsemblBacteria; AFP40963; AFP40963; MSMEI_4509.
DR GeneID; 66735946; -.
DR KEGG; msg:MSMEI_4509; -.
DR KEGG; msm:MSMEG_4626; -.
DR PATRIC; fig|246196.19.peg.4521; -.
DR eggNOG; COG1530; Bacteria.
DR OMA; LQERWNQ; -.
DR OrthoDB; 1209444at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease 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:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
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 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 Coiled coil; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Reference proteome; RNA-binding; rRNA processing;
KW rRNA-binding; tRNA processing; tRNA-binding; Zinc.
FT CHAIN 1..1037
FT /note="Ribonuclease E"
FT /id="PRO_0000429579"
FT DOMAIN 427..504
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 561..589
FT /evidence="ECO:0000255"
FT COMPBIAS 47..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..1008
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 694
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 796
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P21513"
SQ SEQUENCE 1037 AA; 112762 MW; 3B5E50015C058593 CRC64;
MAEDAHTEDL STQTPQQEGL PERLRVHSLA RVLGTTSRRV LDALAEFDGR QRSAHSTVDK
ADAERVRAAL TESPAAETPP EEAPAAETPV ADLVVVQAEQ VEVVTVSEAG PAEPAEPAEP
EAPAAEAEAE AETEVADEAE TPEPTFRGAV LVGDEPESRL ILEHANIPPA RETQTERPDY
LPLFVAPQPV SFEPAVVDDE DEDDDTETGA ESDFDSGADS DSDDDQADRP RRRRRGRRGR
GRGRGEQNDD ATSDADTDST EDQTDGDEQE SGEDSDDSGD EDSTTTEGGT RRRRRRRRRK
SGSGDSDDAV SPDDPPNTVV HERAPRTERS DKSDDSEIQG ISGSTRLEAK RQRRRDGRDA
GRRRPPILSE AEFLARREAV ERTMIVRDKV RTEPPHEGAR YTQIAVLEDG VVVEHFVTSA
ASASLVGNIY LGIVQNVLPS MEAAFVDIGR GRNGVLYAGE VNWEAAGLGG QNRKIEQALK
PGDYVVVQVS KDPVGHKGAR LTTQVSLAGR YLVYVPGASS TGISRKLPDT ERQRLKEILR
EVVPSDAGVI IRTASEGVKE EDIRSDVERL QKRWSEIEAK AAEVTEKKAG AAVALYEEPD
VLVKVIRDLF NEDFSSLIVS GDEAWNTINS YVEAVAPDLM PRLTKYEPAG PDAPDVFAVH
RIDEQLAKAM DRKVWLPSGG TLVIDRTEAM TVVDVNTGKF TGSGGNLEQT VTRNNLEAAE
EIVRQLRLRD IGGIVVIDFI DMVLESNRDL VLRRLTEALA RDRTRHQVSE VTSLGLVQLT
RKRLGTGLVE AFSTACTHCG GRGIVLHGDP IDSASSNGGR KSDSSGGGGS GGGRRGKRGK
KGAARTEEVH VAKVPDHTPG EHPMFKAMAA ANGKHEGDED HEDHEDHETA EDTTAAEVRD
DTRDEHDADE RAHVVTAAVG AAGDEDLDDS DEDSDLDSDE ESDDESDEDE IELDDDEDEL
DEDIEVIGDS DDSDDSDDSD EDDDSDDSDD DSDEDEDSDS DEDEEPVREV YEPPVTAPRA
RVRRRAAARP AGPPSHD
