ID A0A154QEL3_9GAMM Unreviewed; 1052 AA.
AC A0A154QEL3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 08-OCT-2025, entry version 45.
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 ORFNames=RHOFW104T7_17370 {ECO:0000313|EMBL:KZC22585.1};
OS Rhodanobacter thiooxydans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=416169 {ECO:0000313|EMBL:KZC22585.1, ECO:0000313|Proteomes:UP000076131};
RN [1] {ECO:0000313|EMBL:KZC22585.1, ECO:0000313|Proteomes:UP000076131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW104-T7 {ECO:0000313|EMBL:KZC22585.1,
RC ECO:0000313|Proteomes:UP000076131};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
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;
CC Evidence={ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00970};
CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-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 -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000256|ARBA:ARBA00005663}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZC22585.1}.
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DR EMBL; LVJS01000054; KZC22585.1; -; Genomic_DNA.
DR RefSeq; WP_008436178.1; NZ_LVJS01000054.1.
DR AlphaFoldDB; A0A154QEL3; -.
DR STRING; 416169.RHOFW104T7_17370; -.
DR eggNOG; COG1530; Bacteria.
DR Proteomes; UP000076131; Unassembled WGS sequence.
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: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 CDD; cd04453; S1_RNase_E; 1.
DR FunFam; 2.40.50.140:FF:000040; Ribonuclease 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 InterPro; IPR003029; S1_domain.
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 Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00970};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00023136, 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:UP000076131};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00970};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00970};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00970};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00970}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00970}.
FT DOMAIN 39..118
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 402..405
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT REGION 586..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..623
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..725
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..829
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 402
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 405
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 1052 AA; 112206 MW; E4026A69B229908A CRC64;
MKRMLINATQ REELRVAIVD GQNLYDLDIE IPSREQKKSN IYKGRITRVE ASLEACFIEY
GAERHGFLPL KEISREYFTP GLDPHKANIR ELIKEGQEVV VQVEKEERGN KGAALTTFIS
LAGRYMVLMP NNPKAGGVSR RIEGEDRQAL KEALDHVTVP DDVGLIVRTA GLGRDAEELQ
WDLDYLLTLW KSISEAASKQ KAPFLIYQES KLFIRALRDY LRSDIGEILI DDEPLYNDAR
DFMQQVMPNA LRKLKLYRDD TPLFTRYQIE TQIESAFDRQ VRLPSGGSIV IDQTEALTAI
DVNSSKATKG SDIEETAFNT NCEAAVEIAR QARIRDAGGL LVIDFIDMDS PKHQREVEDR
LKDALKLDRA RVQIGRISRF GLLEMSRQRL RPSLGEATQI TCPRCEGHGH IRGVESLSLS
TLRLIEEHAM KDNTGQVLVQ APTSVANFLL NEKRASVVEI ELRHKAHVVI VADEKLETPH
IEIQRIREAD MGEHSKPSYE RLTAVDAVEL PKMGQTLGSG EQPAVSGIVP ASPAPVREEV
AAPVATAAPV VRRQPAAAPA PAPAAAPSGG IISRLFGWFR STEVAAPAPA PKRTDNASDG
SSRNRRDERG NRPGTSSSAS SPRQPRREAA QPGSTKPASA QQARSNRQRS NEVQPRPAPQ
PPSQTAKADR QPRPTTAAES NPARAERKPN PAQPSKVERQ PRVATDERPA VAPPADAANE
AELLLTPPTA SSIPEATDNT ADGEGNQSRR RRGRRGGRRR RRHDEAAADG TGADSTQAEA
LDDEDRDETT ATADVPAARS EPSSHESSPV AAAGEAVPAI PPVRQPTPAQ PNETHAVTPV
ATAASTATPV TTAFNLPPLP PIPESVKSAA ATAAADEHEL VMVAPASTPA PTPTTTTVAV
SSVDTQAAKA DPASAAVVTA VATPTTLSRA ASDTASSAVV AVSGAEPVPT AVTPASSTVA
APSAAATAPA PIASLAHEAS PSTSVAFPAA AAGMPETPVA VQPAVSLPHP KQGDLLAQAG
PQDGLLPSTD DSEAASPQSR GESDAHKGDS NG
//
