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Database: UniProt
Entry: B4TTE9_SALSV
LinkDB: B4TTE9_SALSV
Original site: B4TTE9_SALSV 
ID   B4TTE9_SALSV            Unreviewed;      1067 AA.
AC   B4TTE9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   09-JUL-2014, entry version 34.
DE   RecName: Full=Ribonuclease E;
DE            Short=RNase E;
DE            EC=3.1.26.12;
GN   Name=rne; OrderedLocusNames=SeSA_A1253;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of single-stranded
CC       RNA in A- and U-rich regions.
CC   -!- COFACTOR: Binds 1 Mg(2+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 Zn(2+) ions per homotetramer (By similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
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DR   EMBL; CP001127; ACF92054.1; -; Genomic_DNA.
DR   RefSeq; YP_002114184.1; NC_011094.1.
DR   STRING; 439843.SeSA_A1253; -.
DR   EnsemblBacteria; ACF92054; ACF92054; SeSA_A1253.
DR   PATRIC; 32371163; VBISalEnt87589_1334.
DR   eggNOG; COG1530; -.
DR   HOGENOM; HOG000258027; -.
DR   OMA; ENTKEVH; -.
DR   OrthoDB; EOG6PCPTH; -.
DR   BioCyc; SENT439843:GHHR-3543-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; IPR022967; RNA-binding_domain_S1.
DR   InterPro; IPR028878; RNase_E.
DR   InterPro; IPR004659; RNase_E/G.
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; Complete proteome; Cytoplasm;
KW   Endonuclease; Hydrolase; Magnesium; Membrane; Metal-binding; Nuclease;
KW   RNA-binding; rRNA processing; tRNA processing; Zinc.
FT   DOMAIN       39    119       S1 motif (By similarity).
FT   REGION      404    407       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity (By similarity).
FT   METAL       303    303       Magnesium; catalytic (By
FT                                similarity){EA2}.
FT   METAL       346    346       Magnesium; catalytic (By
FT                                similarity){EA2}.
FT   METAL       404    404       Zinc; shared with dimeric partner (By
FT                                similarity){EA2}.
FT   METAL       407    407       Zinc; shared with dimeric partner (By
FT                                similarity){EA2}.
SQ   SEQUENCE   1067 AA;  119352 MW;  4C8714178CCF61E3 CRC64;
     MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI
     SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALASLEL PEGMGLIVRT AGVGKSAEAL
     QWDLSFRLKH WEAIQKAAES RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVMEMA
     RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT
     AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE
     NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS
     LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKRTAVN AIETRQDGVR CVIVPNDQME
     TPHYSVLRVR KGEETPTLSY MLPKLHEEAM ALPSEEEYAE RKRPEQPALA TFAMPDVPPA
     PTPVEPAVSV ATAKKDNVAA AQPAQPGLFS RFLNALKQLF SGEETKAVET AAPKAEEKAE
     RQQDRRKPRQ NNRRDRNERR DTRDNRAGRD GGESRDDNRR NRRQAQQQNA EARDTRQQET
     AEKVKTGDEQ QQTPRRERSR RRNDDKRQAQ QEVKALNREE LPVQETEQEE RVQQVQPRRK
     QRQLNQKVRF TNSAVVETVD TPVVVDEPRP VENVEQPVPA PRTELAKVDL PVIADIAPEQ
     DDSVEPRDNT GMPRRSRRSP RHLRVSGQRR RRYRDERYPT QSPMPLTVAC ASPEMASGKV
     WIRYPIVRPQ ETQVVEEQRE ADLALPQPVV AEPQVIAATV ALEPQASVQA VENVAVEPQT
     VAEPQVPEVV EVETTHPEVI AAPVDEQPQL IAESDTPVAQ EVIADAEPVA ETADASITVA
     ENVADVVVVE PEEETKAEAA VVEHTAEETV IAPAQVVEKP QDVVCVDDHN HASAPMTRAP
     APEYVPETPH HSDWQRPSFH FEGKGAAGGH SATRVASAPA TRPQPVE
//
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