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Database: UniProt
Entry: B6ZZX1_ECO57
LinkDB: B6ZZX1_ECO57
Original site: B6ZZX1_ECO57 
ID   B6ZZX1_ECO57            Unreviewed;      1061 AA.
AC   B6ZZX1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   26-NOV-2014, entry version 29.
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:EEC26918.1};
GN   ORFNames=ESCCO14588_2915 {ECO:0000313|EMBL:EEC26918.1};
OS   Escherichia coli O157:H7 str. TW14588.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=502346 {ECO:0000313|EMBL:EEC26918.1, ECO:0000313|Proteomes:UP000001326};
RN   [1] {ECO:0000313|EMBL:EEC26918.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TW14588 {ECO:0000313|EMBL:EEC26918.1};
RA   Sebastian Y., Whittam T.S., Manning S.D., Sutton G.;
RL   Submitted (NOV-2008) 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}.
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:EEC26918.1}.
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DR   EMBL; ABKY02000003; EEC26918.1; -; Genomic_DNA.
DR   ProteinModelPortal; B6ZZX1; -.
DR   SMR; B6ZZX1; 1-510.
DR   EnsemblBacteria; EEC26918; EEC26918; ESCCO14588_2915.
DR   PATRIC; 29408149; VBIEscCol82497_2823.
DR   OMA; ENTKEVH; -.
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:UP000001326};
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:EEC26918.1};
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   1061 AA;  118273 MW;  C5D6382C7DCF033A CRC64;
     MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI
     SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALASLEL PEGMGLIVRT AGVGKSAEAL
     QWDLSFRLKH WEAIKKAAES RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA
     RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT
     AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE
     NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS
     LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKRSAVN AIETRQDGVR CVIVPNDQME
     TPHYHVLRVR KGEETPTLSY MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA
     PTPAEPAAPV VAPAPKAAPA TPATPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA
     KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT AETREGRQQA
     EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE EQSVQETEQE ERVRPVQPRR
     KQRQLNQKVR YEQSVAEETV VAPVAEETVA AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ
     QEENNADNRD NGGMPRRSRR SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG
     KVWIRYPIVR PQDVQVEEQR EQEEVQVQPM VTEVPVAAAV EPVVSAPVVE EMAEVVEAPV
     PVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEHAEPVVEP QEETADIEEV
     AETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVTAVKPEIT VEHNHATAPM TRAPAPEYVP
     EAPRHSDWQR PTFAFEGKGA AGGHTATHHA SAAPARPQPV E
//
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