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Protein

50S ribosomal protein L25

Gene

rplY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10885-MONOMER.
ECOL316407:JW2173-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L25
Gene namesi
Name:rplY
Ordered Locus Names:b2185, JW2173
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10885. rplY.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 949450S ribosomal protein L25PRO_0000181478Add
BLAST

Proteomic databases

PaxDbiP68919.
PRIDEiP68919.

2D gel databases

SWISS-2DPAGEP68919.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaKP0A6Y81EBI-553087,EBI-542092

Protein-protein interaction databases

DIPiDIP-35885N.
IntActiP68919. 13 interactions.
MINTiMINT-1261165.
STRINGi511145.b2185.

Structurei

Secondary structure

1
94
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi6 – 83Combined sources
Helixi14 – 229Combined sources
Beta strandi25 – 317Combined sources
Beta strandi33 – 353Combined sources
Beta strandi38 – 436Combined sources
Helixi44 – 507Combined sources
Helixi54 – 574Combined sources
Beta strandi61 – 655Combined sources
Beta strandi72 – 798Combined sources
Beta strandi81 – 844Combined sources
Beta strandi86 – 938Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B75NMR-A1-94[»]
1D6KNMR-A1-94[»]
1DFUX-ray1.80P1-94[»]
1ML5electron microscopy14.00v1-94[»]
2J28electron microscopy8.00V1-94[»]
2RDOelectron microscopy9.10V1-94[»]
3BBXelectron microscopy10.00V1-94[»]
3J5Lelectron microscopy6.60V1-94[»]
3J7Zelectron microscopy3.90V1-94[»]
3J9Yelectron microscopy3.90V1-94[»]
487Delectron microscopy7.50N1-94[»]
4CSUelectron microscopy5.50W1-94[»]
4U1UX-ray2.95BV/DV1-94[»]
4U1VX-ray3.00BV/DV1-94[»]
4U20X-ray2.90BV/DV1-94[»]
4U24X-ray2.90BV/DV1-94[»]
4U25X-ray2.90BV/DV1-94[»]
4U26X-ray2.80BV/DV1-94[»]
4U27X-ray2.80BV/DV1-94[»]
4UY8electron microscopy3.8081-94[»]
4V47electron microscopy12.30AT1-94[»]
4V48electron microscopy11.50AT1-94[»]
4V4HX-ray3.46BV/DV1-94[»]
4V4QX-ray3.46BV/DV1-94[»]
4V4Velectron microscopy15.00BT1-94[»]
4V4Welectron microscopy15.00BT1-94[»]
4V50X-ray3.22BV/DV1-94[»]
4V52X-ray3.21BV/DV1-94[»]
4V53X-ray3.54BV/DV1-94[»]
4V54X-ray3.30BV/DV1-94[»]
4V55X-ray4.00BV/DV1-94[»]
4V56X-ray3.93BV/DV1-94[»]
4V57X-ray3.50BV/DV1-94[»]
4V5BX-ray3.74AV/CV1-94[»]
4V5Helectron microscopy5.80BW1-94[»]
4V5YX-ray4.45BV/DV1-94[»]
4V64X-ray3.50BV/DV1-94[»]
4V65electron microscopy9.00BC1-94[»]
4V66electron microscopy9.00BC1-94[»]
4V69electron microscopy6.70BV1-94[»]
4V6CX-ray3.19BV/DV1-94[»]
4V6DX-ray3.81BV/DV1-94[»]
4V6EX-ray3.71BV/DV1-94[»]
4V6Kelectron microscopy8.25AW1-94[»]
4V6Lelectron microscopy13.20BW1-94[»]
4V6Melectron microscopy7.10BV1-94[»]
4V6Nelectron microscopy12.10AX1-94[»]
4V6Oelectron microscopy14.70BX1-94[»]
4V6Pelectron microscopy13.50BX1-94[»]
4V6Qelectron microscopy11.50BX1-94[»]
4V6Relectron microscopy11.50BX1-94[»]
4V6Selectron microscopy13.10AX1-94[»]
4V6Telectron microscopy8.30BV1-94[»]
4V6Velectron microscopy9.80BZ1-94[»]
4V6Yelectron microscopy12.00BV1-94[»]
4V6Zelectron microscopy12.00BV1-94[»]
4V70electron microscopy17.00BV1-94[»]
4V71electron microscopy20.00BV1-94[»]
4V72electron microscopy13.00BV1-94[»]
4V73electron microscopy15.00BV1-94[»]
4V74electron microscopy17.00BV1-94[»]
4V75electron microscopy12.00BV1-94[»]
4V76electron microscopy17.00BV1-94[»]
4V77electron microscopy17.00BV1-94[»]
4V78electron microscopy20.00BV1-94[»]
4V79electron microscopy15.00BV1-94[»]
4V7Aelectron microscopy9.00BV1-94[»]
4V7Belectron microscopy6.80BV1-94[»]
4V7Celectron microscopy7.60BX1-94[»]
4V7Delectron microscopy7.60AY1-94[»]
4V7Ielectron microscopy9.60AV1-94[»]
4V7SX-ray3.25BV/DV1-94[»]
4V7TX-ray3.19BV/DV1-94[»]
4V7UX-ray3.10BV/DV1-94[»]
4V7VX-ray3.29BV/DV1-94[»]
4V85X-ray3.20Z1-94[»]
4V89X-ray3.70BZ1-94[»]
4V9CX-ray3.30BV/DV1-94[»]
4V9DX-ray3.00CV/DV1-94[»]
4V9OX-ray2.90AV/CV/EV/GV1-94[»]
4V9PX-ray2.90AV/CV/EV/GV1-94[»]
4WF1X-ray3.09BV/DV1-94[»]
4WWWX-ray3.10RV/YV1-94[»]
4YBBX-ray2.10CW/DW1-94[»]
5AFIelectron microscopy2.90V1-94[»]
5AKAelectron microscopy5.70V1-94[»]
ProteinModelPortaliP68919.
SMRiP68919. Positions 1-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68919.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L25P family.Curated

Phylogenomic databases

eggNOGiCOG1825.
HOGENOMiHOG000277629.
KOiK02897.
OMAiHAGKFPA.
OrthoDBiEOG6SZ1PC.
PhylomeDBiP68919.

Family and domain databases

Gene3Di2.40.240.10. 1 hit.
HAMAPiMF_01336. Ribosomal_L25.
InterProiIPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR029751. Ribosomal_L25.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR020055. Ribosomal_L25_short.
[Graphical view]
PfamiPF01386. Ribosomal_L25p. 1 hit.
[Graphical view]
ProDomiPD012503. Ribosomal_L25. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50715. SSF50715. 1 hit.

Sequencei

Sequence statusi: Complete.

P68919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTINAEVRK EQGKGASRRL RAANKFPAII YGGKEAPLAI ELDHDKVMNM
60 70 80 90
QAKAEFYSEV LTIVVDGKEI KVKAQDVQRH PYKPKLQHID FVRA
Length:94
Mass (Da):10,693
Last modified:July 21, 1986 - v1
Checksum:i85DAF5ACBA1C5F86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 949LQHIDFVRA → CSTSTSFALNC in AAA16413 (Ref. 6) Curated

Mass spectrometryi

Molecular mass is 10693.4 Da from positions 1 - 94. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13326 Genomic DNA. Translation: BAA02585.1.
U00008 Genomic DNA. Translation: AAA16413.1.
U00096 Genomic DNA. Translation: AAC75246.1.
AP009048 Genomic DNA. Translation: BAE76650.1.
PIRiS16002. R5EC25.
RefSeqiNP_416690.1. NC_000913.3.
WP_000494183.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75246; AAC75246; b2185.
BAE76650; BAE76650; BAE76650.
GeneIDi945618.
KEGGieco:b2185.
PATRICi32119725. VBIEscCol129921_2273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13326 Genomic DNA. Translation: BAA02585.1.
U00008 Genomic DNA. Translation: AAA16413.1.
U00096 Genomic DNA. Translation: AAC75246.1.
AP009048 Genomic DNA. Translation: BAE76650.1.
PIRiS16002. R5EC25.
RefSeqiNP_416690.1. NC_000913.3.
WP_000494183.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B75NMR-A1-94[»]
1D6KNMR-A1-94[»]
1DFUX-ray1.80P1-94[»]
1ML5electron microscopy14.00v1-94[»]
2J28electron microscopy8.00V1-94[»]
2RDOelectron microscopy9.10V1-94[»]
3BBXelectron microscopy10.00V1-94[»]
3J5Lelectron microscopy6.60V1-94[»]
3J7Zelectron microscopy3.90V1-94[»]
3J9Yelectron microscopy3.90V1-94[»]
487Delectron microscopy7.50N1-94[»]
4CSUelectron microscopy5.50W1-94[»]
4U1UX-ray2.95BV/DV1-94[»]
4U1VX-ray3.00BV/DV1-94[»]
4U20X-ray2.90BV/DV1-94[»]
4U24X-ray2.90BV/DV1-94[»]
4U25X-ray2.90BV/DV1-94[»]
4U26X-ray2.80BV/DV1-94[»]
4U27X-ray2.80BV/DV1-94[»]
4UY8electron microscopy3.8081-94[»]
4V47electron microscopy12.30AT1-94[»]
4V48electron microscopy11.50AT1-94[»]
4V4HX-ray3.46BV/DV1-94[»]
4V4QX-ray3.46BV/DV1-94[»]
4V4Velectron microscopy15.00BT1-94[»]
4V4Welectron microscopy15.00BT1-94[»]
4V50X-ray3.22BV/DV1-94[»]
4V52X-ray3.21BV/DV1-94[»]
4V53X-ray3.54BV/DV1-94[»]
4V54X-ray3.30BV/DV1-94[»]
4V55X-ray4.00BV/DV1-94[»]
4V56X-ray3.93BV/DV1-94[»]
4V57X-ray3.50BV/DV1-94[»]
4V5BX-ray3.74AV/CV1-94[»]
4V5Helectron microscopy5.80BW1-94[»]
4V5YX-ray4.45BV/DV1-94[»]
4V64X-ray3.50BV/DV1-94[»]
4V65electron microscopy9.00BC1-94[»]
4V66electron microscopy9.00BC1-94[»]
4V69electron microscopy6.70BV1-94[»]
4V6CX-ray3.19BV/DV1-94[»]
4V6DX-ray3.81BV/DV1-94[»]
4V6EX-ray3.71BV/DV1-94[»]
4V6Kelectron microscopy8.25AW1-94[»]
4V6Lelectron microscopy13.20BW1-94[»]
4V6Melectron microscopy7.10BV1-94[»]
4V6Nelectron microscopy12.10AX1-94[»]
4V6Oelectron microscopy14.70BX1-94[»]
4V6Pelectron microscopy13.50BX1-94[»]
4V6Qelectron microscopy11.50BX1-94[»]
4V6Relectron microscopy11.50BX1-94[»]
4V6Selectron microscopy13.10AX1-94[»]
4V6Telectron microscopy8.30BV1-94[»]
4V6Velectron microscopy9.80BZ1-94[»]
4V6Yelectron microscopy12.00BV1-94[»]
4V6Zelectron microscopy12.00BV1-94[»]
4V70electron microscopy17.00BV1-94[»]
4V71electron microscopy20.00BV1-94[»]
4V72electron microscopy13.00BV1-94[»]
4V73electron microscopy15.00BV1-94[»]
4V74electron microscopy17.00BV1-94[»]
4V75electron microscopy12.00BV1-94[»]
4V76electron microscopy17.00BV1-94[»]
4V77electron microscopy17.00BV1-94[»]
4V78electron microscopy20.00BV1-94[»]
4V79electron microscopy15.00BV1-94[»]
4V7Aelectron microscopy9.00BV1-94[»]
4V7Belectron microscopy6.80BV1-94[»]
4V7Celectron microscopy7.60BX1-94[»]
4V7Delectron microscopy7.60AY1-94[»]
4V7Ielectron microscopy9.60AV1-94[»]
4V7SX-ray3.25BV/DV1-94[»]
4V7TX-ray3.19BV/DV1-94[»]
4V7UX-ray3.10BV/DV1-94[»]
4V7VX-ray3.29BV/DV1-94[»]
4V85X-ray3.20Z1-94[»]
4V89X-ray3.70BZ1-94[»]
4V9CX-ray3.30BV/DV1-94[»]
4V9DX-ray3.00CV/DV1-94[»]
4V9OX-ray2.90AV/CV/EV/GV1-94[»]
4V9PX-ray2.90AV/CV/EV/GV1-94[»]
4WF1X-ray3.09BV/DV1-94[»]
4WWWX-ray3.10RV/YV1-94[»]
4YBBX-ray2.10CW/DW1-94[»]
5AFIelectron microscopy2.90V1-94[»]
5AKAelectron microscopy5.70V1-94[»]
ProteinModelPortaliP68919.
SMRiP68919. Positions 1-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35885N.
IntActiP68919. 13 interactions.
MINTiMINT-1261165.
STRINGi511145.b2185.

Chemistry

ChEMBLiCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP68919.

Proteomic databases

PaxDbiP68919.
PRIDEiP68919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75246; AAC75246; b2185.
BAE76650; BAE76650; BAE76650.
GeneIDi945618.
KEGGieco:b2185.
PATRICi32119725. VBIEscCol129921_2273.

Organism-specific databases

EchoBASEiEB0878.
EcoGeneiEG10885. rplY.

Phylogenomic databases

eggNOGiCOG1825.
HOGENOMiHOG000277629.
KOiK02897.
OMAiHAGKFPA.
OrthoDBiEOG6SZ1PC.
PhylomeDBiP68919.

Enzyme and pathway databases

BioCyciEcoCyc:EG10885-MONOMER.
ECOL316407:JW2173-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68919.
PROiP68919.

Family and domain databases

Gene3Di2.40.240.10. 1 hit.
HAMAPiMF_01336. Ribosomal_L25.
InterProiIPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR029751. Ribosomal_L25.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR020055. Ribosomal_L25_short.
[Graphical view]
PfamiPF01386. Ribosomal_L25p. 1 hit.
[Graphical view]
ProDomiPD012503. Ribosomal_L25. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50715. SSF50715. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of the 5S RNA binding protein L25 from Escherichia coli ribosomes."
    Dovgas N.V., Markova L.F., Mednikova T.A., Vinokurov L.M., Alakhov Y.B., Ovchinnikov Y.A.
    FEBS Lett. 53:351-354(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: MRE-600.
  2. Cited for: SEQUENCE REVISION.
  3. "The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes."
    Bitar K.G., Wittmann-Liebold B.
    Hoppe-Seyler's Z. Physiol. Chem. 356:1343-1352(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K12.
  4. "Primary structure of the protein L25 from the ribosomes of E. coli MRE-600 forming part of the 5S-RNA-protein complex."
    Alakhov Y.B., Vinokurov L.M., Dovgas N.V., Markova L.F., Mednikova T.A., Motuz L.P., Kashparov I.A., Ovchinnikov Y.A.
    Bioorg. Khim. 2:5-18(1976)
    Cited for: PROTEIN SEQUENCE.
    Strain: MRE-600.
  5. "Cloning, characterization, and physical location of the rplY gene which encodes ribosomal protein L25 in Escherichia coli K12."
    Uemura Y., Isono S., Isono K.
    Mol. Gen. Genet. 226:341-344(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  6. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / BHB2600.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "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.
  9. "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.
  10. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10.
    Strain: K12.
  11. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT, BINDING TO 5S RRNA.
    Strain: K12.
  12. "Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli."
    Spierer P., Zimmermann R.A.
    Biochemistry 17:2474-2479(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FORMATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
    Strain: MRE-600.
  13. "5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins."
    Shpanchenko O.V., Zvereva M.I., Dontsova O.A., Nierhaus K.H., Bogdanov A.A.
    FEBS Lett. 394:71-75(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
    Strain: K12 / A19.
  14. "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.
  15. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  16. "The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases."
    Stoldt M., Woehnert J., Goerlach M., Brown L.R.
    EMBO J. 17:6377-6384(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH A FRAGMENT OF 5S RRNA.
    Strain: MRE-600.
  17. "The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition."
    Stoldt M., Woehnert J., Ohlenschlaeger O., Goerlach M., Brown L.R.
    EMBO J. 18:6508-6521(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH A FRAGMENT OF 5S RRNA.
  18. "Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution."
    Lu M., Steitz T.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:2023-2028(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) BOUND TO A FRAGMENT OF 5S RRNA.
  19. "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
    Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
    J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  20. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  22. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL25_ECOLI
AccessioniPrimary (citable) accession number: P68919
Secondary accession number(s): P02426, Q2MAQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 110 of the entry and version 1 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.