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P05055

- PNP_ECOLI

UniProt

P05055 - PNP_ECOLI

Protein

Polyribonucleotide nucleotidyltransferase

Gene

pnp

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Also involved, along with RNase II, in tRNA processing.5 PublicationsUniRule annotation

    Catalytic activityi

    RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.3 PublicationsUniRule annotation

    Cofactori

    Magnesium. Can also use manganese.1 PublicationUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi486 – 4861Magnesium
    Metal bindingi492 – 4921Magnesium

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: EcoCyc
    2. cyclic-di-GMP binding Source: EcoCyc
    3. identical protein binding Source: IntAct
    4. magnesium ion binding Source: UniProtKB-HAMAP
    5. polyribonucleotide nucleotidyltransferase activity Source: EcoCyc
    6. protein binding Source: IntAct
    7. RNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. mRNA catabolic process Source: UniProtKB-HAMAP
    2. response to heat Source: EcoCyc
    3. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    4. RNA processing Source: InterPro

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Magnesium, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10743-MONOMER.
    ECOL316407:JW5851-MONOMER.
    MetaCyc:EG10743-MONOMER.
    BRENDAi2.7.7.8. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyribonucleotide nucleotidyltransferaseUniRule annotation (EC:2.7.7.8UniRule annotation)
    Alternative name(s):
    Polynucleotide phosphorylaseUniRule annotation
    Short name:
    PNPaseUniRule annotation
    Gene namesi
    Name:pnpUniRule annotation
    Ordered Locus Names:b3164, JW5851
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10743. pnp.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation
    Note: Has also been isolated in association with the inner membrane.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 802RR → AA: Strongly reduces RNA binding. Reduces RNA degradation.
    Mutagenesisi83 – 831R → A: No effect on RNA-binding. No effect on degradation of long RNA molecules. Impairs degradation of short RNA molecules. 1 Publication
    Mutagenesisi100 – 1001R → D: Abolishes enzyme activity. 1 Publication
    Mutagenesisi319 – 3191R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi398 – 3992RR → DD: Abolishes enzyme activity.
    Mutagenesisi428 – 4281V → P: Abolishes enzyme activity. 1 Publication
    Mutagenesisi444 – 4441C → W: Abolishes enzyme activity. 1 Publication
    Mutagenesisi492 – 4921D → G: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 711711Polyribonucleotide nucleotidyltransferasePRO_0000197913Add
    BLAST

    Proteomic databases

    PaxDbiP05055.
    PRIDEiP05055.

    2D gel databases

    SWISS-2DPAGEP05055.

    PTM databases

    PhosSiteiP0810422.

    Expressioni

    Inductioni

    Expression is negatively autoregulated at the translational level via an RNase III-dependent mechanism. At low temperature, the destabilizing effect of PNPase on its own mRNA is less efficient, leading to a decrease in repression and an increase in the expression level.2 Publications

    Gene expression databases

    GenevestigatoriP05055.

    Interactioni

    Subunit structurei

    Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Interacts with RNase E (rne). Homotrimer. The homotrimer forms a ring-like structure with a central channel, where RNA molecules can bind. RNA molecules bind between neighboring subunits.6 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-548080,EBI-548080
    rhlBP0A8J86EBI-548080,EBI-555806
    rneP2151311EBI-548080,EBI-549958

    Protein-protein interaction databases

    DIPiDIP-10522N.
    IntActiP05055. 45 interactions.
    MINTiMINT-244786.
    STRINGi511145.b3164.

    Structurei

    Secondary structure

    1
    711
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi14 – 2310
    Beta strandi27 – 359
    Beta strandi38 – 469
    Beta strandi59 – 657
    Helixi67 – 704
    Helixi86 – 9914
    Helixi100 – 1023
    Beta strandi111 – 1199
    Helixi126 – 14116
    Beta strandi152 – 1576
    Beta strandi160 – 1645
    Helixi169 – 1724
    Beta strandi174 – 1818
    Beta strandi186 – 19611
    Helixi198 – 21114
    Helixi213 – 22513
    Helixi242 – 2443
    Turni247 – 2504
    Helixi251 – 2577
    Helixi263 – 28422
    Helixi290 – 31122
    Turni315 – 3184
    Beta strandi327 – 3326
    Beta strandi337 – 3459
    Beta strandi348 – 3569
    Beta strandi375 – 3817
    Helixi384 – 3874
    Helixi402 – 41211
    Beta strandi418 – 4214
    Beta strandi425 – 4339
    Helixi438 – 45215
    Beta strandi462 – 47110
    Beta strandi474 – 4807
    Helixi483 – 4886
    Beta strandi490 – 4978
    Beta strandi502 – 5098
    Helixi516 – 54025
    Beta strandi623 – 63311
    Beta strandi636 – 6405
    Beta strandi642 – 6443
    Helixi662 – 6654
    Beta strandi671 – 6788
    Beta strandi686 – 6894

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SRONMR-A617-692[»]
    3CDIX-ray2.60A2-711[»]
    3CDJX-ray2.80A2-547[»]
    3GCMX-ray2.50A/B/C1-549[»]
    3GLLX-ray2.70A1-549[»]
    3GMEX-ray2.40A1-549[»]
    3H1CX-ray3.57A/B/C/G/I/K/M/O/R/T/V/X1-549[»]
    ProteinModelPortaliP05055.
    SMRiP05055. Positions 1-692.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05055.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini553 – 61260KHUniRule annotationAdd
    BLAST
    Domaini622 – 69069S1 motifUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni77 – 804FFRR loop; important for RNA binding
    Regioni327 – 3315Interaction with RNase E

    Domaini

    The S1 motif domain is important for trimerization and RNA-binding.1 Publication

    Sequence similaritiesi

    Belongs to the polyribonucleotide nucleotidyltransferase family.UniRule annotation
    Contains 1 KH domain.UniRule annotation
    Contains 1 S1 motif domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1185.
    HOGENOMiHOG000218327.
    KOiK00962.
    OMAiPRWDWVA.
    OrthoDBiEOG6WT8CC.
    PhylomeDBiP05055.

    Family and domain databases

    Gene3Di1.10.10.400. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1370.10. 1 hit.
    3.30.230.70. 2 hits.
    HAMAPiMF_01595. PNPase.
    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    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.
    [Graphical view]
    PANTHERiPTHR11252. PTHR11252. 1 hit.
    PfamiPF00013. KH_1. 1 hit.
    PF03726. PNPase. 1 hit.
    PF01138. RNase_PH. 2 hits.
    PF03725. RNase_PH_C. 2 hits.
    PF00575. S1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005499. PNPase. 1 hit.
    SMARTiSM00322. KH. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF46915. SSF46915. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54211. SSF54211. 2 hits.
    SSF54791. SSF54791. 1 hit.
    SSF55666. SSF55666. 2 hits.
    TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05055-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA    50
    KPGQDFFPLT VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPIR 100
    PLFPEGFVNE VQVIATVVSV NPQVNPDIVA MIGASAALSL SGIPFNGPIG 150
    AARVGYINDQ YVLNPTQDEL KESKLDLVVA GTEAAVLMVE SEAQLLSEDQ 200
    MLGAVVFGHE QQQVVIQNIN ELVKEAGKPR WDWQPEPVNE ALNARVAALA 250
    EARLSDAYRI TDKQERYAQV DVIKSETIAT LLAEDETLDE NELGEILHAI 300
    EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA 350
    LVTATLGTAR DAQVLDELMG ERTDTFLFHY NFPPYSVGET GMVGSPKRRE 400
    IGHGRLAKRG VLAVMPDMDK FPYTVRVVSE ITESNGSSSM ASVCGASLAL 450
    MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD ILGDEDHLGD MDFKVAGSRD 500
    GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA INAPRGDISE 550
    FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT 600
    DGEKAKHAIR RIEEITAEIE VGRVYTGKVT RIVDFGAFVA IGGGKEGLVH 650
    ISQIADKRVE KVTDYLQMGQ EVPVKVLEVD RQGRIRLSIK EATEQSQPAA 700
    APEAPAAEQG E 711
    Length:711
    Mass (Da):77,101
    Last modified:November 1, 1995 - v3
    Checksum:i785B7D54716FC2DE
    GO

    Sequence cautioni

    The sequence AAA57967.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAE77210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti357 – 3571G → R in AAA83905. (PubMed:2432069)Curated
    Sequence conflicti450 – 4501L → S in AAA83905. (PubMed:2432069)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02638 Genomic DNA. Translation: AAA83905.1.
    U18997 Genomic DNA. Translation: AAA57967.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76198.2.
    AP009048 Genomic DNA. Translation: BAE77210.1. Different initiation.
    X00761 Genomic DNA. Translation: CAA25332.1.
    M14425 Genomic DNA. Translation: AAA24596.1.
    PIRiH65106.
    RefSeqiNP_417633.4. NC_000913.3.
    YP_491351.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76198; AAC76198; b3164.
    BAE77210; BAE77210; BAE77210.
    GeneIDi12933437.
    947672.
    KEGGiecj:Y75_p3086.
    eco:b3164.
    PATRICi32121746. VBIEscCol129921_3259.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02638 Genomic DNA. Translation: AAA83905.1 .
    U18997 Genomic DNA. Translation: AAA57967.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC76198.2 .
    AP009048 Genomic DNA. Translation: BAE77210.1 . Different initiation.
    X00761 Genomic DNA. Translation: CAA25332.1 .
    M14425 Genomic DNA. Translation: AAA24596.1 .
    PIRi H65106.
    RefSeqi NP_417633.4. NC_000913.3.
    YP_491351.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SRO NMR - A 617-692 [» ]
    3CDI X-ray 2.60 A 2-711 [» ]
    3CDJ X-ray 2.80 A 2-547 [» ]
    3GCM X-ray 2.50 A/B/C 1-549 [» ]
    3GLL X-ray 2.70 A 1-549 [» ]
    3GME X-ray 2.40 A 1-549 [» ]
    3H1C X-ray 3.57 A/B/C/G/I/K/M/O/R/T/V/X 1-549 [» ]
    ProteinModelPortali P05055.
    SMRi P05055. Positions 1-692.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10522N.
    IntActi P05055. 45 interactions.
    MINTi MINT-244786.
    STRINGi 511145.b3164.

    PTM databases

    PhosSitei P0810422.

    2D gel databases

    SWISS-2DPAGE P05055.

    Proteomic databases

    PaxDbi P05055.
    PRIDEi P05055.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76198 ; AAC76198 ; b3164 .
    BAE77210 ; BAE77210 ; BAE77210 .
    GeneIDi 12933437.
    947672.
    KEGGi ecj:Y75_p3086.
    eco:b3164.
    PATRICi 32121746. VBIEscCol129921_3259.

    Organism-specific databases

    EchoBASEi EB0736.
    EcoGenei EG10743. pnp.

    Phylogenomic databases

    eggNOGi COG1185.
    HOGENOMi HOG000218327.
    KOi K00962.
    OMAi PRWDWVA.
    OrthoDBi EOG6WT8CC.
    PhylomeDBi P05055.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10743-MONOMER.
    ECOL316407:JW5851-MONOMER.
    MetaCyc:EG10743-MONOMER.
    BRENDAi 2.7.7.8. 2026.

    Miscellaneous databases

    EvolutionaryTracei P05055.
    PROi P05055.

    Gene expression databases

    Genevestigatori P05055.

    Family and domain databases

    Gene3Di 1.10.10.400. 1 hit.
    2.40.50.140. 1 hit.
    3.30.1370.10. 1 hit.
    3.30.230.70. 2 hits.
    HAMAPi MF_01595. PNPase.
    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    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.
    [Graphical view ]
    PANTHERi PTHR11252. PTHR11252. 1 hit.
    Pfami PF00013. KH_1. 1 hit.
    PF03726. PNPase. 1 hit.
    PF01138. RNase_PH. 2 hits.
    PF03725. RNase_PH_C. 2 hits.
    PF00575. S1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005499. PNPase. 1 hit.
    SMARTi SM00322. KH. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46915. SSF46915. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF54211. SSF54211. 2 hits.
    SSF54791. SSF54791. 1 hit.
    SSF55666. SSF55666. 2 hits.
    TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1."
      Regnier P., Grunberg-Manago M., Portier C.
      J. Biol. Chem. 262:63-68(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions."
      Portier C., Regnier P.
      Nucleic Acids Res. 12:6091-6102(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-196.
    5. "Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli."
      Evans S., Dennis P.P.
      Gene 40:15-22(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    7. "Purification and properties of polynucleotide phosphorylase from Escherichia coli."
      Kimhi Y., Littauer U.Z.
      J. Biol. Chem. 243:231-240(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    8. "Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure."
      Portier C.
      FEBS Lett. 50:79-81(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "E.coli polynucleotide phosphorylase expression is autoregulated through an RNase III-dependent mechanism."
      Robert-Le Meur M., Portier C.
      EMBO J. 11:2633-2641(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "The role of individual exoribonucleases in processing at the 3' end of Escherichia coli tRNA precursors."
      Li Z., Deutscher M.P.
      J. Biol. Chem. 269:6064-6071(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRNA PROCESSING.
    11. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    12. "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome."
      Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C., Krisch H.M., Carpousis A.J.
      Genes Dev. 12:2770-2781(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNE.
    13. "Increased expression of Escherichia coli polynucleotide phosphorylase at low temperatures is linked to a decrease in the efficiency of autocontrol."
      Mathy N., Jarrige A.C., Robert-Le Meur M., Portier C.
      J. Bacteriol. 183:3848-3854(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. "Mutational analysis of polynucleotide phosphorylase from Escherichia coli."
      Jarrige A., Brechemier-Baey D., Mathy N., Duche O., Portier C.
      J. Mol. Biol. 321:397-409(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ARG-100; ARG-319; VAL-428; CYS-444 AND ASP-492.
    15. "Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'."
      Prud'homme-Genereux A., Beran R.K., Iost I., Ramey C.S., Mackie G.A., Simons R.W.
      Mol. Microbiol. 54:1409-1421(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNE, ASSOCIATION WITH RNA DEGRADOSOME.
      Strain: CF881.
    16. Cited for: SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    17. "RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome."
      Taghbalout A., Rothfield L.
      J. Biol. Chem. 283:13850-13855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNE AND RHLB.
    18. "The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold."
      Bycroft M., Hubbard T.J., Proctor M., Freund S.M., Murzin A.G.
      Cell 88:235-242(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 617-692.
    19. "Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation."
      Shi Z., Yang W.Z., Lin-Chao S., Chak K.F., Yuan H.S.
      RNA 14:2361-2371(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, RNA-BINDING, DOMAIN, MUTAGENESIS OF 79-ARG-ARG-80 AND ARG-83.
    20. "Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly."
      Nurmohamed S., Vaidialingam B., Callaghan A.J., Luisi B.F.
      J. Mol. Biol. 389:17-33(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-549 IN COMPLEXES WITH RNASE E; RNA AND MANGANESE IONS, FUNCTION, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiPNP_ECOLI
    AccessioniPrimary (citable) accession number: P05055
    Secondary accession number(s): P78109, Q2M946
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3