CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004967
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease R 
Protein Synonyms/Alias
 RNase R; Protein VacB 
Gene Name
 rnr 
Gene Synonyms/Alias
 vacB; yjeC; b4179; JW5741 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
13FQEREAEKYANPIPSacetylation[1]
30FILEHLTKREKPASRacetylation[1]
86PERLDLVKGTVIGHRacetylation[1]
105FLRVEGRKDDLYLSSacetylation[1]
249EQQVAGLKEEVPEEAacetylation[1]
287DDAVYCEKKRGGGWRacetylation[1]
369KGRLTGYKFYEAVMSacetylation[1]
385HARLTYTKVWHILQGacetylation[1]
405EQYAPLVKHLEELHNacetylation[1]
415EELHNLYKVLDKAREacetylation[1]
488ALFRIHDKPSTEAITacetylation[1]
513LELPGGNKPEPRDYAacetylation[1]
544TMLLRSMKQAIYDPEacetylation[1, 2]
719AVNMDERKIDFSLISacetylation[1]
773DSAFRGEKKTKPKAAacetylation[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] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842
Functional Description
 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (rRNAs, tRNAs and SsrA/tmRNA). In stationary phase, involved in the post-transcriptional regulation of ompA mRNA stability. Shortens RNA processively to di- and trinucleotides. In vitro, exhibits helicase activity, which is independent of its RNase activity. Required for the expression of virulence genes in enteroinvasive strains of E.coli. 
Sequence Annotation
 DOMAIN 644 725 S1 motif.
 MOD_RES 544 544 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding; Stress response; Virulence. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 813 AA 
Protein Sequence
MSQDPFQERE AEKYANPIPS REFILEHLTK REKPASRDEL AVELHIEGEE QLEGLRRRLR 60
AMERDGQLVF TRRQCYALPE RLDLVKGTVI GHRDGYGFLR VEGRKDDLYL SSEQMKTCIH 120
GDQVLAQPLG ADRKGRREAR IVRVLVPKTS QIVGRYFTEA GVGFVVPDDS RLSFDILIPP 180
DQIMGARMGF VVVVELTQRP TRRTKAVGKI VEVLGDNMGT GMAVDIALRT HEIPYIWPQA 240
VEQQVAGLKE EVPEEAKAGR VDLRDLPLVT IDGEDARDFD DAVYCEKKRG GGWRLWVAIA 300
DVSYYVRPST PLDREARNRG TSVYFPSQVI PMLPEVLSNG LCSLNPQVDR LCMVCEMTVS 360
SKGRLTGYKF YEAVMSSHAR LTYTKVWHIL QGDQDLREQY APLVKHLEEL HNLYKVLDKA 420
REERGGISFE SEEAKFIFNA ERRIERIEQT QRNDAHKLIE ECMILANISA ARFVEKAKEP 480
ALFRIHDKPS TEAITSFRSV LAELGLELPG GNKPEPRDYA ELLESVADRP DAEMLQTMLL 540
RSMKQAIYDP ENRGHFGLAL QSYAHFTSPI RRYPDLTLHR AIKYLLAKEQ GHQGNTTETG 600
GYHYSMEEML QLGQHCSMAE RRADEATRDV ADWLKCDFML DQVGNVFKGV ISSVTGFGFF 660
VRLDDLFIDG LVHVSSLDND YYRFDQVGQR LMGESSGQTY RLGDRVEVRV EAVNMDERKI 720
DFSLISSERA PRNVGKTARE KAKKGDAGKK GGKRRQVGKK VNFEPDSAFR GEKKTKPKAA 780
KKDARKAKKP SAKTQKIAAA TKAKRAAKKK VAE 813 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0034458; F:3'-5' RNA helicase activity; IDA:EcoCyc.
 GO:0000175; F:3'-5'-exoribonuclease activity; IDA:EcoCyc.
 GO:0008859; F:exoribonuclease II activity; IEA:HAMAP.
 GO:0008997; F:ribonuclease R activity; IDA:EcoCyc.
 GO:0003723; F:RNA binding; IEA:HAMAP.
 GO:0006402; P:mRNA catabolic process; IMP:EcoCyc.
 GO:0034470; P:ncRNA processing; IMP:EcoCyc.
 GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
 GO:0009409; P:response to cold; IEP:EcoCyc. 
Interpro
 IPR011129; Cold_shock_prot.
 IPR012340; NA-bd_OB-fold.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR022967; RNA-binding_domain_S1.
 IPR013223; RNase_B_OB_dom.
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS.
 IPR004476; RNase_II/RNase_R.
 IPR011805; RNase_R.
 IPR013668; RNase_R_HTH_12. 
Pfam
 PF08461; HTH_12
 PF08206; OB_RNB
 PF00773; RNB
 PF00575; S1 
SMART
 SM00357; CSP
 SM00955; RNB
 SM00316; S1 
PROSITE
 PS01175; RIBONUCLEASE_II
 PS50126; S1 
PRINTS