CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004969
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease E 
Protein Synonyms/Alias
 RNase E 
Gene Name
 rne 
Gene Synonyms/Alias
 ams; hmp1; b1084; JW1071 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
37ESPGHEQKKANIYKGacetylation[1]
71RHGFLPLKEIAREYFacetylation[1]
91AHGRPNIKDVLREGQacetylation[1]
106EVIVQIDKEERGNKGacetylation[1]
175VRTAGVGKSAEALQWacetylation[1]
195LKHWEAIKKAAESRPacetylation[1]
235EILIDNPKVLELARQacetylation[1]
255GRPDFSSKIKLYTGEacetylation[1]
433LIEEEALKENTQEVHacetylation[1]
455ASYLLNEKRSAVNAIacetylation[1]
589FSGGEETKPTEQPAPacetylation[1]
601PAPKAEAKPERQQDRacetylation[1, 2]
695RQAQQEAKALNVEEQacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
Functional Description
 Matures 5S rRNA from its precursors from all the rRNA genes. It also cleaves RNA I, a molecule that controls the replication of colE1 plasmid DNA. It is the major endoribonuclease participating in mRNA turnover in E.coli. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process. 
Sequence Annotation
 DOMAIN 39 119 S1 motif.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1061 AA 
Protein Sequence
MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY 60
GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI 120
SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALASLEL PEGMGLIVRT AGVGKSAEAL 180
QWDLSFRLKH WEAIKKAAES RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA 240
RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT 300
AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE 360
NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS 420
LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKRSAVN AIETRQDGVR CVIVPNDQME 480
TPHYHVLRVR KGEETPTLSY MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA 540
PTPAEPAAPV VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA 600
KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT AETRESRQQA 660
EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE EQSVQETEQE ERVRPVQPRR 720
KQRQLNQKVR YEQSVAEEAV VAPVVEETVA AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ 780
QEENNADNRD NGGMPRRSRR SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG 840
KVWIRYPIVR PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV 900
QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP QEETADIEEV 960
VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT VEHNHATAPM TRAPAPEYVP 1020
EAPRHSDWQR PTFAFEGKGA AGGHTATHHA SAAPARPQPV E 1061 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoCyc.
 GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO:0004540; F:ribonuclease activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0006401; P:RNA catabolic process; IDA:EcoCyc.
 GO:0000967; P:rRNA 5'-end processing; IMP:EcoCyc. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR021968; PNPase_C.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR019307; RNA-bd_AU-1/RNase_E/G.
 IPR022967; RNA-binding_domain_S1.
 IPR004659; RNase_E/G. 
Pfam
 PF12111; PNPase_C
 PF10150; RNase_E_G
 PF00575; S1 
SMART
 SM00316; S1 
PROSITE
 PS50126; S1 
PRINTS