RNE_HAEIN
ID RNE_HAEIN Reviewed; 935 AA.
AC P44443;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=HI_0413;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SUBCELLULAR LOCATION, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=22509045; DOI=10.1073/pnas.1120181109;
RA Murashko O.N., Kaberdin V.R., Lin-Chao S.;
RT "Membrane binding of Escherichia coli RNase E catalytic domain stabilizes
RT protein structure and increases RNA substrate affinity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7019-7024(2012).
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,
CC ECO:0000269|PubMed:22509045}. Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00970, ECO:0000269|PubMed:22509045}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00970}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_00970}. Note=Associated with the inner
CC membrane via the N-terminal region (residues 1-418), subcellular
CC locations shown upon expression in E.coli.
CC {ECO:0000269|PubMed:22509045}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00970}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22072.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22072.1; ALT_INIT; Genomic_DNA.
DR PIR; E64066; E64066.
DR RefSeq; NP_438575.2; NC_000907.1.
DR RefSeq; WP_010868984.1; NC_000907.1.
DR AlphaFoldDB; P44443; -.
DR SMR; P44443; -.
DR STRING; 71421.HI_0413; -.
DR PRIDE; P44443; -.
DR EnsemblBacteria; AAC22072; AAC22072; HI_0413.
DR KEGG; hin:HI_0413; -.
DR PATRIC; fig|71421.8.peg.433; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_1_0_6; -.
DR PhylomeDB; P44443; -.
DR BioCyc; HINF71421:G1GJ1-428-MON; -.
DR BRENDA; 3.1.26.12; 2529.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004540; F:ribonuclease activity; IBA:GO_Central.
DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA 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; IBA:GO_Central.
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; IPR021968; PNPase_C.
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; PF12111; PNPase_C; 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; Reference proteome;
KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing; Zinc.
FT CHAIN 1..935
FT /note="Ribonuclease E"
FT /id="PRO_0000097375"
FT DOMAIN 39..119
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT REGION 403..406
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT REGION 571..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 403
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 406
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 935 AA; 106584 MW; 1493239989920023 CRC64;
MKRMLINATQ KEELRVALVD GQRLFDLDIE SPGHEQKKAN IYKGKITRVE PSLEAAFVDY
GAERHGFLPL KEIAREYFPD DYVFQGRPNI RDILVEGQEV IVQVNKEERG NKGAALTTFV
SLAGSYLVLM PNNPRAGGIS RRIEGDERTE LKEALSSLDV PDGVGLIVRT AGVGKSPEEL
QWDLKVLLHH WEAIKQASQS RPAPFLIHQE SDVIVRAIRD YLRRDIGEIL IDSPKIFEKA
KEHIKLVRPD FINRVKLYQG EVPLFSHYQI ESQIESAFQR EVRLPSGGSI VIDVTEALTA
IDINSARSTR GGDIEETALN TNLEAADEIA RQLRLRDLGG LVVIDFIDMT PIRHQREVEN
RIRDAVRPDR ARIQISRISR FGLLEMSRQR LSPSLGESSH HICPRCQGTG KVRDNESLSL
SILRLLEEEA LKENTKQVHT IVPVQIASYL LNEKRKAISN IEKRHNVDII VAPNEAMETP
HFSVFRLRDG EEVNELSYNL AKIHCAQDEN TEESLLSRNV ETTAVIEQPA VESAVVALSI
SEAAPTPVER KSNEPSLLAK IIAKIKGLFA TKSEENKPKN NRTSRNPNRN QRRSQDRRSS
RRPRSENNET ERTEEQVRNV RERNQRRPRR NLVEESIAES AVNSTPVFEA KEERTEPVTQ
RRQRRDLRKR VRVEDNETVV ENNFSTTEKM PEVDVITVQN NDEKPVHQNQ RSERQERQRR
TPRHLRAANN QRRRRDQEPK SPMPLFAAVV SPELASGKAW IDYSTVNLPK ENHFLSVDEL
LEQEKTKKGF ITPAMGIVVE EKSPDVKPAL DFITQPANES VQKKVQESLD RLSSYKPQEV
VESIDPAINV DEPETLEKVS KFVRTYEFNG RLGTISSVPH TKAEMTLAKA NDEMPEDFPI
RAWQDSRYYF YGKGAAGHHC AISHVYSEPT RTKSE
