ID   A0A366AP74_9VIBR        Unreviewed;      1052 AA.
AC   A0A366AP74;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   05-DEC-2018, entry version 2.
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=DLR71_03550 {ECO:0000313|EMBL:RBM65075.1};
OS   Vibrio sp. 2017V-1105.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=2204203 {ECO:0000313|EMBL:RBM65075.1, ECO:0000313|Proteomes:UP000252343};
RN   [1] {ECO:0000313|EMBL:RBM65075.1, ECO:0000313|Proteomes:UP000252343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2017V-1105 {ECO:0000313|EMBL:RBM65075.1,
RC   ECO:0000313|Proteomes:UP000252343};
RA   Islam M.T., Liang K., Im M.S., Winkjer J., Busby S., Batra D.,
RA   Rowe L., Tarr C.L., Boucher Y.;
RT   "Draft genome sequences of nine Vibrio sp. clinical isolates from
RT   across the United States representing the closest known relative of
RT   Vibrio cholerae.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that plays a central role in RNA
CC       processing and decay. Required for the maturation of 5S and 16S
CC       rRNAs and the majority of tRNAs. Also involved in the degradation
CC       of most mRNAs. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and
CC         U-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-
CC       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: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation. Within
CC       the RNA degradosome, Rnase E assembles into a homotetramer formed
CC       by a dimer of dimers. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}.
CC       Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic
CC       side {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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RBM65075.1}.
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DR   EMBL; QKKT01000003; RBM65075.1; -; Genomic_DNA.
DR   Proteomes; UP000252343; Unassembled WGS sequence.
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   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 {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Complete proteome {ECO:0000313|Proteomes:UP000252343};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   DOMAIN       39    119       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      403    406       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   METAL       302    302       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       345    345       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       403    403       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       406    406       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   1052 AA;  117526 MW;  1195AC75400546F1 CRC64;
     MKRMLINATQ KEELRVALVD GQRLFDLDIE SPGHESKKAN IYKGRITRIE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPD GYSYQGRPNI KDVLNEGQEV IVQIEKEERG SKGAALTTFI
     SLAGSYLVLM PNNPRAGGIS RRIEGDERTE LKSALSSLEL PQGMGLIVRT AGVGKSAEEL
     EWDLNVLLKH WSAIKQASDS NPAPFLIHQE SNVIVRAIRD YLRRDIGEIL IDSNSIYERA
     LEHIRLVRPD FVNRVKKYEG EVPLFSHFQI ESQIESAFQR EVRLPSGGSI VIDPTEALTS
     IDINSARATK GGDIEETALN TNLEAADEIA RQLRLRDLGG LVVIDFIDMT PVRHQREVEN
     RLREAVRVDR ARVQIGRISR FGLLEMSRQR LSPSLAEASH HICPRCKGTG VIRDNESLAL
     SVLRLIEEEA LKDNTSQVLA VVPVSIASYL LNEKRRSINH IEKAQQVRIT IVPNSDMETP
     HFEVIRVREG EEQDVLSYLI PKKLEAMKEA EGKEVVDVEL KPKRIEEPVL KGFAAPAEAV
     PAPTPKPKAE PQPVAEVQQP AQPGFFSRVF KAIASLFSAT PEAAKVEAPV TQNSEQDKPR
     RERNERNNDR RRNPRDKNRR RGNEENNERN DKETSNNNRK PQERKPKQER GERNERNDRN
     ERPETERPER QDRRNKRDES KTAKLLEQGR QLAAEAQQEV KAVEPKEEKA AVVKERRQRR
     KLSKQIRVKD QLAAEELDNL STAPVDNAFD APAPVNLPVT DDFSDSAQED NEQDDQKQRR
     NRRSPRHLRA SGQRRRRGRD RRPNPFRLRK GGVASPEMAM GKVMPRYDLA PRPQSRHETA
     EGAQHVTHVT PTAATAVVES EKVAAPRVLG GVAFPEMAMG KVIVCRETAA VQPEPVVQEP
     VITDVIAETL IAPVEPVVVE AAVIEAPVIE ESATETAALE TVVAKVAEVE EPAKISDEVV
     AQTTVEVIAD KMAEPIKVVK PVTVSATSLT AKAVIQQPYA SSPMTKAPGS DDIREVQVNA
     APLRAERYQA RGAGSQVARN QASAGMSKPQ SF
//