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Database: UniProt
Entry: C9Y0Z7_CROTZ
LinkDB: C9Y0Z7_CROTZ
Original site: C9Y0Z7_CROTZ 
ID   C9Y0Z7_CROTZ            Unreviewed;      1062 AA.
AC   C9Y0Z7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   26-NOV-2014, entry version 31.
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   ECO:0000313|EMBL:CBA29936.1};
GN   OrderedLocusNames=Ctu_16630 {ECO:0000313|EMBL:CBA29936.1};
GN   ORFNames=CTU_16630 {ECO:0000313|EMBL:CBA29936.1};
OS   Cronobacter turicensis (strain DSM 18703 / LMG 23827 / z3032).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216 {ECO:0000313|Proteomes:UP000002069};
RN   [1] {ECO:0000313|Proteomes:UP000002069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / LMG 23827 / z3032
RC   {ECO:0000313|Proteomes:UP000002069};
RA   Tischler P., Lehner A., Rattei T., Stephan R.;
RT   "The complete genome sequence of Cronobacter turicensis.";
RL   Submitted (AUG-2009) 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: Endonucleolytic cleavage of single-stranded
CC       RNA in A- and U-rich regions. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- COFACTOR:
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- COFACTOR:
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   -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP-
CC       Rule:MF_00970}.
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DR   EMBL; FN543093; CBA29936.1; -; Genomic_DNA.
DR   RefSeq; YP_003210026.1; NC_013282.2.
DR   STRING; 413502.Ctu_16630; -.
DR   EnsemblBacteria; CBA29936; CBA29936; CTU_16630.
DR   GeneID; 8459016; -.
DR   KEGG; ctu:CTU_16630; -.
DR   PATRIC; 20403957; VBICroTur2449_1578.
DR   HOGENOM; HOG000258027; -.
DR   KO; K08300; -.
DR   OMA; ENTKEVH; -.
DR   OrthoDB; EOG6PCPTH; -.
DR   BioCyc; CTUR693216:GI0P-1719-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP.
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; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
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   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 {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002069};
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   ECO:0000313|EMBL:CBA29936.1};
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:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   REGION      404    407       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   METAL       303    303       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       346    346       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       404    404       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       407    407       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   1062 AA;  117973 MW;  1E359A5D92A03FAC CRC64;
     MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPA SYASHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI
     SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALSSLEL PDGMGLIVRT AGVGKSAEAL
     QWDLSFRLKH WEAIQKAAEN RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA
     RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDTTEALT
     AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE
     NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS
     LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKREAIT AIETRQGGVR CVIVPNDQME
     TPHYSVLRVR KGEETHTLSY MLPKLHEEAM ALPSEEEYAE RKRPEQPALA TFVMPDVPPM
     PQETSAPAAE PAAPKAPVKA AEPAKEGFLS RAISALKSLF ASEPQAQPVA SEPEPQPAKN
     REDKPQDRRN GRRQNNRRDR NERGERSERG ERPSRENRDN RDNRDNSEAR EENRRNRREK
     QQQNAETREV RAPVAEEVAE KPKSRDDQQQ SPRRDRNRRR SEEKRQAQQE VNVLNRDDAV
     EETEQEDRVV QVMPRRKPRQ LSQKVRIESA AEAAAVGNTD APVAETREEA APLALPANVE
     TPAAAEDNNQ TGSENAGMPR RSRRSPRHLR VSGQRRRRYR DERYPTQSPM PLTVACASPE
     MASGKVWIRY PLPRVQEQEE QQLEQNTAPV AETQTTEAPV APVTDAVVVE PSAVESAPQE
     TVVETTYPEA ISTPVDAQPQ IIEPQDEAVA QQVAQNAVAA DAPVAEDAPR EEAAAVMAES
     APEEAPQPEA IADEPVKTPE AAPVVAPNAQ ETEVKAPVVA VASASVASAP MTRAPAPDYV
     PEPPRHSDWV RPTFDFSGKG SAGGHSATHQ ASAPATRPQP VE
//
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