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UniProtKB/Swiss-Prot entry P21513


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RNE_ECOLI
Primary accession number P21513
Secondary accession number P77591
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on August 29, 2003 (Sequence version 6)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Ribonuclease E
Synonyms RNase E
EC 3.1.26.12
Gene name
Name: rne
Synonyms: ams, hmp1
OrderedLocusNames: b1084, JW1071
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1025.
STRAIN=K12;
DOI=10.1016/0022-2836(92)90489-7; PubMed=1447789 [NCBI, ExPASy, EBI, Israel, Japan]
Casaregola S., Jacq A., Laoudj D., McGurk G., Margarson S., Tempete M., Norris V., Holland I.B.;
"Cloning and analysis of the entire Escherichia coli ams gene. ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein.";
J. Mol. Biol. 228:30-40(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-844.
STRAIN=K12;
PubMed=1704367 [NCBI, ExPASy, EBI, Israel, Japan]
Claverie-Martin F., Diaz-Torres M., Yancey S.D., Kushner S.R.;
"Analysis of the altered mRNA stability (ams) gene from Escherichia coli. Nucleotide sequence, transcriptional analysis, and homology of its product to MRP3, a mitochondrial ribosomal protein from Neurospora crassa.";
J. Biol. Chem. 266:2843-2851(1991).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-27.
STRAIN=K12;
DOI=10.1093/nar/19.1.125; PubMed=2011493 [NCBI, ExPASy, EBI, Israel, Japan]
Chauhan A.K., Miczak A., Taraseviciene L., Apirion D.;
"Sequencing and expression of the rne gene of Escherichia coli.";
Nucleic Acids Res. 19:125-129(1991).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 844-1061, AND CHARACTERIZATION.
STRAIN=K12;
PubMed=8415644 [NCBI, ExPASy, EBI, Israel, Japan]
Cormack R.S., Genereaux J.L., Mackie G.A.;
"RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product.";
Proc. Natl. Acad. Sci. U.S.A. 90:9006-9010(1993).
[8]
CHARACTERIZATION.
DOI=10.1093/nar/29.9.1864; PubMed=11328869 [NCBI, ExPASy, EBI, Israel, Japan]
Walsh A.P., Tock M.R., Mallen M.H., Kaberdin V.R., Gabain Av A., McDowall K.J.;
"Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli.";
Nucleic Acids Res. 29:1864-1871(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U00096; AAC74168.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X67470; CAA47818.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M62747; AAA23443.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54309; CAA38206.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L23942; AAA03347.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A64852; S27311.
RefSeq AP_001710.1; -.
NP_415602.1; -.
3D structure databases
PDB
1SLJ; NMR; -; A=35-125.[ExPASy / RCSB / EBI]
1SMX; X-ray; 1.80 A; A/B=35-125.[ExPASy / RCSB / EBI]
1SN8; X-ray; 2.00 A; A/B=35-125.[ExPASy / RCSB / EBI]
2BX2; X-ray; 2.85 A; L=1-510.[ExPASy / RCSB / EBI]
2C0B; X-ray; 3.18 A; L=1-510.[ExPASy / RCSB / EBI]
2C4R; X-ray; 3.60 A; L=1-510.[ExPASy / RCSB / EBI]
2FYM; X-ray; 1.60 A; B/E=833-850.[ExPASy / RCSB / EBI]
2VMK; X-ray; 3.30 A; A/B/C/D=1-515.[ExPASy / RCSB / EBI]
2VRT; X-ray; 3.50 A; A/B/C/D=1-509.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1SLJ; -.
1SMX; -.
1SN8; -.
2BX2; -.
2C0B; -.
2C4R; -.
2FYM; -.
2VMK; -.
2VRT; -.
DisProt DP00207; -.
ModBase P21513.
Protein-protein interaction databases
DIP DIP:10727N; -.
IntAct P21513; -.
Enzyme and pathway databases
BioCyc EcoCyc:EG10859-MON; -.
Organism-specific databases
EchoBASE EB0852; -.
EcoGene EG10859; rne.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004519; Molecular function: endonuclease activity (inferred from electronic annotation from UniProtKB-KW).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004540; Molecular function: ribonuclease activity (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0006396; Biological process: RNA processing (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR012340; NA-bd_OB-fold.
IPR004659; RNaseE/G.
IPR003029; S1_RNA-bd.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
Pfam PF00575; S1; 1.
Pfam graphical view of domain structure.
SMART SM00316; S1; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00757; RNaseEG; 1.
PROSITE PS50126; S1; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P21513.
Genome annotation databases
GeneID 945641; -.
GenomeReviews U00096_GR; b1084.
AP009048_GR; JW1071.
KEGG ecj:JW1071; -.
eco:b1084; -.
Phylogenomic databases
HOGENOM P21513; -.
Genome annotation databases
CMR P21513; b1084.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1061  1061     Ribonuclease E. PRO_0000097373
DOMAIN   39    119  81     S1 motif. 
CONFLICT   390    390        Q -> H (in Ref. 5; AAA23443). 
CONFLICT   487    487        L -> V (in Ref. 4 and 5). 
CONFLICT   564    564        A -> R (in Ref. 4; CAA47818). 
CONFLICT   784    784        N -> K (in Ref. 4; CAA47818). 
CONFLICT   838    838        A -> R (in Ref. 5). 
CONFLICT   905    905        P -> R (in Ref. 4; CAA47818). 
CONFLICT   1048   1048        H -> R (in Ref. 7; AAA03347). 
STRAND   2      7  6      
STRAND   14     20  7      
STRAND   23     30  8      
STRAND   42     50  9      
HELIX   51     53  3      
STRAND   55     64  10      
STRAND   66     69  4      
HELIX   70     72  3      
HELIX   75     77  3      
STRAND   84     86  3      
HELIX   90     92  3      
STRAND   99    106  8      
STRAND   115    118  4      
HELIX   151    155  5      
STRAND   165    168  4      
HELIX   170    174  5      
HELIX   177    199  23      
STRAND   205    208  4      
HELIX   213    221  9      
STRAND   226    232  7      
HELIX   234    246  13      
HELIX   250    255  6      
STRAND   256    258  3      
HELIX   265    268  4      
HELIX   272    277  6      
STRAND   281    284  4      
STRAND   290    295  6      
STRAND   300    305  6      
HELIX   315    336  22      
STRAND   341    346  6      
HELIX   353    366  14      
TURN   367    369  3      
STRAND   374    379  6      
STRAND   383    389  7      
HELIX   396    400  5      
STRAND   401    403  3      
STRAND   405    414  10      
HELIX   416    432  17      
STRAND   436    443  8      
HELIX   445    451  7      
TURN   452    455  4      
HELIX   456    465  10      
TURN   466    468  3      
STRAND   470    475  6      
STRAND   485    490  6      
HELIX   499    501  3      
HELIX   502    506  5      
TURN   507    509  3      
HELIX   835    838  4      
Sequence information
Length: 1061 AA [This is the length of the unprocessed precursor] Molecular weight: 118197 Da [This is the MW of the unprocessed precursor] CRC64: D4066D80E1DE7D37 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY 

        70         80         90        100        110        120 
GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI 

       130        140        150        160        170        180 
SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALASLEL PEGMGLIVRT AGVGKSAEAL 

       190        200        210        220        230        240 
QWDLSFRLKH WEAIKKAAES RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA 

       250        260        270        280        290        300 
RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT 

       310        320        330        340        350        360 
AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE 

       370        380        390        400        410        420 
NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS 

       430        440        450        460        470        480 
LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKRSAVN AIETRQDGVR CVIVPNDQME 

       490        500        510        520        530        540 
TPHYHVLRVR KGEETPTLSY MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA 

       550        560        570        580        590        600 
PTPAEPAAPV VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA 

       610        620        630        640        650        660 
KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT AETRESRQQA 

       670        680        690        700        710        720 
EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE EQSVQETEQE ERVRPVQPRR 

       730        740        750        760        770        780 
KQRQLNQKVR YEQSVAEEAV VAPVVEETVA AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ 

       790        800        810        820        830        840 
QEENNADNRD NGGMPRRSRR SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG 

       850        860        870        880        890        900 
KVWIRYPIVR PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV 

       910        920        930        940        950        960 
QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP QEETADIEEV 

       970        980        990       1000       1010       1020 
VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT VEHNHATAPM TRAPAPEYVP 

      1030       1040       1050       1060 
EAPRHSDWQR PTFAFEGKGA AGGHTATHHA SAAPARPQPV E 

P21513 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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