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P05055

- PNP_ECOLI

UniProt

P05055 - PNP_ECOLI

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Protein

Polyribonucleotide nucleotidyltransferase

Gene

pnp

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Mg2+1 PublicationUniRule annotation, Mn2+1 PublicationUniRule annotationNote: 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. 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 802RR → AA: Strongly reduces RNA binding. Reduces RNA degradation. 1 Publication
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 – 117Combined sources
Beta strandi14 – 2310Combined sources
Beta strandi27 – 359Combined sources
Beta strandi38 – 469Combined sources
Beta strandi59 – 657Combined sources
Helixi67 – 704Combined sources
Helixi86 – 9914Combined sources
Helixi100 – 1023Combined sources
Beta strandi111 – 1199Combined sources
Helixi126 – 14116Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi160 – 1645Combined sources
Helixi169 – 1724Combined sources
Beta strandi174 – 1818Combined sources
Beta strandi186 – 19611Combined sources
Helixi198 – 21114Combined sources
Helixi213 – 22513Combined sources
Helixi242 – 2443Combined sources
Turni247 – 2504Combined sources
Helixi251 – 2577Combined sources
Helixi263 – 28422Combined sources
Helixi290 – 31122Combined sources
Turni315 – 3184Combined sources
Beta strandi327 – 3326Combined sources
Beta strandi337 – 3459Combined sources
Beta strandi348 – 3569Combined sources
Beta strandi375 – 3817Combined sources
Helixi384 – 3874Combined sources
Helixi402 – 41211Combined sources
Beta strandi418 – 4214Combined sources
Beta strandi425 – 4339Combined sources
Helixi438 – 45215Combined sources
Beta strandi462 – 47110Combined sources
Beta strandi474 – 4807Combined sources
Helixi483 – 4886Combined sources
Beta strandi490 – 4978Combined sources
Beta strandi502 – 5098Combined sources
Helixi516 – 54025Combined sources
Beta strandi623 – 63311Combined sources
Beta strandi636 – 6405Combined sources
Beta strandi642 – 6443Combined sources
Helixi662 – 6654Combined sources
Beta strandi671 – 6788Combined sources
Beta strandi686 – 6894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP05055.
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. S1_dom.
[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

        10         20         30         40         50
MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA
60 70 80 90 100
KPGQDFFPLT VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPIR
110 120 130 140 150
PLFPEGFVNE VQVIATVVSV NPQVNPDIVA MIGASAALSL SGIPFNGPIG
160 170 180 190 200
AARVGYINDQ YVLNPTQDEL KESKLDLVVA GTEAAVLMVE SEAQLLSEDQ
210 220 230 240 250
MLGAVVFGHE QQQVVIQNIN ELVKEAGKPR WDWQPEPVNE ALNARVAALA
260 270 280 290 300
EARLSDAYRI TDKQERYAQV DVIKSETIAT LLAEDETLDE NELGEILHAI
310 320 330 340 350
EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA
360 370 380 390 400
LVTATLGTAR DAQVLDELMG ERTDTFLFHY NFPPYSVGET GMVGSPKRRE
410 420 430 440 450
IGHGRLAKRG VLAVMPDMDK FPYTVRVVSE ITESNGSSSM ASVCGASLAL
460 470 480 490 500
MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD ILGDEDHLGD MDFKVAGSRD
510 520 530 540 550
GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA INAPRGDISE
560 570 580 590 600
FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
610 620 630 640 650
DGEKAKHAIR RIEEITAEIE VGRVYTGKVT RIVDFGAFVA IGGGKEGLVH
660 670 680 690 700
ISQIADKRVE KVTDYLQMGQ EVPVKVLEVD RQGRIRLSIK EATEQSQPAA
710
APEAPAAEQG E
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.Curated
The sequence BAE77210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P05055.
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. S1_dom.
[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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 160 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

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