CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002209
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polyribonucleotide nucleotidyltransferase 
Protein Synonyms/Alias
 Polynucleotide phosphorylase; PNPase 
Gene Name
 pnp 
Gene Synonyms/Alias
 b3164; JW5851 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
171NPTQDELKESKLDLVacetylation[1]
263DAYRITDKQERYAQVacetylation[1, 2]
302EILHAIEKNVVRSRVacetylation[3]
397TGMVGSPKRREIGHGacetylation[1]
420AVMPDMDKFPYTVRVacetylation[1]
494HLGDMDFKVAGSRDGacetylation[1]
516IKIEGITKEIMQVALacetylation[1, 2]
527QVALNQAKGARLHILacetylation[2]
566KINPDKIKDVIGKGGacetylation[1]
571KIKDVIGKGGSVIRAacetylation[1]
604IAATDGEKAKHAIRRacetylation[1]
606ATDGEKAKHAIRRIEacetylation[1]
657HISQIADKRVEKVTDacetylation[1]
661IADKRVEKVTDYLQMacetylation[1]
675MGQEVPVKVLEVDRQacetylation[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]
 [3] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 
Functional Description
 Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction. 
Sequence Annotation
 DOMAIN 553 612 KH.
 DOMAIN 622 690 S1 motif.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotidyltransferase; Reference proteome; RNA-binding; Stress response; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 711 AA 
Protein Sequence
MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA KPGQDFFPLT 60
VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPIR PLFPEGFVNE VQVIATVVSV 120
NPQVNPDIVA MIGASAALSL SGIPFNGPIG AARVGYINDQ YVLNPTQDEL KESKLDLVVA 180
GTEAAVLMVE SEAQLLSEDQ MLGAVVFGHE QQQVVIQNIN ELVKEAGKPR WDWQPEPVNE 240
ALNARVAALA EARLSDAYRI TDKQERYAQV DVIKSETIAT LLAEDETLDE NELGEILHAI 300
EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA LVTATLGTAR 360
DAQVLDELMG ERTDTFLFHY NFPPYSVGET GMVGSPKRRE IGHGRLAKRG VLAVMPDMDK 420
FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD 480
ILGDEDHLGD MDFKVAGSRD GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA 540
INAPRGDISE FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT 600
DGEKAKHAIR RIEEITAEIE VGRVYTGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE 660
KVTDYLQMGQ EVPVKVLEVD RQGRIRLSIK EATEQSQPAA APEAPAAEQG E 711 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0000175; F:3'-5'-exoribonuclease activity; IDA:EcoCyc.
 GO:0035438; F:cyclic-di-GMP binding; IDA:EcoCyc.
 GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IDA:EcoCyc.
 GO:0003723; F:RNA binding; IEA:HAMAP.
 GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR001247; ExoRNase_PH_dom1.
 IPR015847; ExoRNase_PH_dom2.
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1.
 IPR009019; KH_prok-type.
 IPR012340; NA-bd_OB-fold.
 IPR012162; PNPase.
 IPR027408; PNPase/RNase_PH_dom.
 IPR015848; PNPase_PH_RNA-bd_bac/org-type.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR022967; RNA-binding_domain_S1. 
Pfam
 PF00013; KH_1
 PF03726; PNPase
 PF01138; RNase_PH
 PF03725; RNase_PH_C
 PF00575; S1 
SMART
 SM00322; KH
 SM00316; S1 
PROSITE
 PS50084; KH_TYPE_1
 PS50126; S1 
PRINTS