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P68919

- RL25_ECOLI

UniProt

P68919 - RL25_ECOLI

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Protein
50S ribosomal protein L25
Gene
rplY, b2185, JW2173
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation

GO - Molecular functioni

  1. 5S rRNA binding Source: InterPro
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10885. rplY.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 949450S ribosomal protein L25UniRule annotation
PRO_0000181478Add
BLAST

Proteomic databases

PaxDbiP68919.
PRIDEiP68919.

2D gel databases

SWISS-2DPAGEP68919.

Expressioni

Gene expression databases

GenevestigatoriP68919.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA.1 Publication

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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi6 – 83
Helixi14 – 229
Beta strandi25 – 317
Beta strandi33 – 353
Beta strandi38 – 436
Helixi44 – 507
Helixi54 – 574
Beta strandi61 – 655
Beta strandi66 – 683
Beta strandi72 – 798
Beta strandi81 – 844
Beta strandi86 – 938

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B75NMR-A1-94[»]
1D6KNMR-A1-94[»]
1DFUX-ray1.80P1-94[»]
1ML5electron microscopy14.00v1-94[»]
1P85electron microscopy12.30T1-94[»]
1P86electron microscopy11.50T1-94[»]
1VS6X-ray3.46V1-94[»]
1VS8X-ray3.46V1-94[»]
1VT2X-ray3.30V1-94[»]
2AW4X-ray3.46V1-94[»]
2AWBX-ray3.46V1-94[»]
2GYAelectron microscopy15.00T1-94[»]
2GYCelectron microscopy15.00T1-94[»]
2I2TX-ray3.22V1-94[»]
2I2VX-ray3.22V1-94[»]
2J28electron microscopy8.00V1-94[»]
2QAMX-ray3.21V1-94[»]
2QAOX-ray3.21V1-94[»]
2QBAX-ray3.54V1-94[»]
2QBCX-ray3.54V1-94[»]
2QBEX-ray3.30V1-94[»]
2QBGX-ray3.30V1-94[»]
2QBIX-ray4.00V1-94[»]
2QBKX-ray4.00V1-94[»]
2QOVX-ray3.93V1-94[»]
2QOXX-ray3.93V1-94[»]
2QOZX-ray3.50V1-94[»]
2QP1X-ray3.50V1-94[»]
2RDOelectron microscopy9.10V1-94[»]
2VHMX-ray3.74V1-94[»]
2VHNX-ray3.74V1-94[»]
2WWQelectron microscopy5.80W1-94[»]
2Z4LX-ray4.45V1-94[»]
2Z4NX-ray4.45V1-94[»]
3BBXelectron microscopy10.00V1-94[»]
3DF2X-ray3.50V1-94[»]
3DF4X-ray3.50V1-94[»]
3E1Belectron microscopy-C1-94[»]
3E1Delectron microscopy-C1-94[»]
3FIKelectron microscopy6.70V1-94[»]
3I1NX-ray3.19V1-94[»]
3I1PX-ray3.19V1-94[»]
3I1RX-ray3.81V1-94[»]
3I1TX-ray3.81V1-94[»]
3I20X-ray3.71V1-94[»]
3I22X-ray3.71V1-94[»]
3IZTelectron microscopy-W1-94[»]
3IZUelectron microscopy-W1-94[»]
3J01electron microscopy-V1-94[»]
3J0Telectron microscopy12.10X1-94[»]
3J0Welectron microscopy14.70X1-94[»]
3J0Yelectron microscopy13.50X1-94[»]
3J11electron microscopy13.10X1-94[»]
3J12electron microscopy11.50X1-94[»]
3J14electron microscopy11.50X1-94[»]
3J19electron microscopy8.30V1-94[»]
3J37electron microscopy9.80Z1-94[»]
3J4Xelectron microscopy12.00V1-94[»]
3J50electron microscopy20.00V1-94[»]
3J51electron microscopy17.00V1-94[»]
3J52electron microscopy12.00V1-94[»]
3J54electron microscopy13.00V1-94[»]
3J56electron microscopy15.00V1-94[»]
3J58electron microscopy17.00V1-94[»]
3J5Aelectron microscopy12.00V1-94[»]
3J5Celectron microscopy17.00V1-94[»]
3J5Eelectron microscopy17.00V1-94[»]
3J5Gelectron microscopy20.00V1-94[»]
3J5Ielectron microscopy15.00V1-94[»]
3J5Kelectron microscopy9.00V1-94[»]
3J5Lelectron microscopy6.60V1-94[»]
3J5Oelectron microscopy6.80V1-94[»]
3J5Uelectron microscopy7.60X1-94[»]
3J5Welectron microscopy7.60Y1-94[»]
3KCRelectron microscopy-V1-94[»]
3OASX-ray3.25V1-94[»]
3OATX-ray3.25V1-94[»]
3OFCX-ray3.19V1-94[»]
3OFDX-ray3.19V1-94[»]
3OFQX-ray3.10V1-94[»]
3OFRX-ray3.10V1-94[»]
3OFZX-ray3.29V1-94[»]
3OG0X-ray3.29V1-94[»]
3ORBX-ray3.30V1-94[»]
3R8SX-ray3.00V1-94[»]
3R8TX-ray3.00V1-94[»]
3SGFX-ray3.20Z1-94[»]
3UOSX-ray3.70Z1-94[»]
487Delectron microscopy7.50N1-94[»]
4CSUelectron microscopy5.50W1-94[»]
4GARX-ray3.30V1-94[»]
4GAUX-ray3.30V1-94[»]
4KIXX-ray2.90V1-94[»]
4KIZX-ray2.90V1-94[»]
4KJ1X-ray2.90V1-94[»]
4KJ3X-ray2.90V1-94[»]
4KJ5X-ray2.90V1-94[»]
4KJ7X-ray2.90V1-94[»]
4KJ9X-ray2.90V1-94[»]
4KJBX-ray2.90V1-94[»]
ProteinModelPortaliP68919.
SMRiP68919. Positions 1-94.

Miscellaneous databases

EvolutionaryTraceiP68919.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1825.
HOGENOMiHOG000277629.
KOiK02897.
OMAiSIELDHD.
OrthoDBiEOG6SZ1PC.
PhylomeDBiP68919.

Family and domain databases

Gene3Di2.40.240.10. 1 hit.
HAMAPiMF_01336. Ribosomal_L25.
InterProiIPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR020055. Ribosomal_L25_short.
[Graphical view]
SUPFAMiSSF50715. SSF50715. 1 hit.

Sequencei

Sequence statusi: Complete.

P68919-1 [UniParc]FASTAAdd to Basket

« Hide

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

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 949LQHIDFVRA → CSTSTSFALNC in AAA16413. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_490425.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75246; AAC75246; b2185.
BAE76650; BAE76650; BAE76650.
GeneIDi12934501.
945618.
KEGGiecj:Y75_p2148.
eco:b2185.
PATRICi32119725. VBIEscCol129921_2273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S16002. R5EC25.
RefSeqi NP_416690.1. NC_000913.3.
YP_490425.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B75 NMR - A 1-94 [» ]
1D6K NMR - A 1-94 [» ]
1DFU X-ray 1.80 P 1-94 [» ]
1ML5 electron microscopy 14.00 v 1-94 [» ]
1P85 electron microscopy 12.30 T 1-94 [» ]
1P86 electron microscopy 11.50 T 1-94 [» ]
1VS6 X-ray 3.46 V 1-94 [» ]
1VS8 X-ray 3.46 V 1-94 [» ]
1VT2 X-ray 3.30 V 1-94 [» ]
2AW4 X-ray 3.46 V 1-94 [» ]
2AWB X-ray 3.46 V 1-94 [» ]
2GYA electron microscopy 15.00 T 1-94 [» ]
2GYC electron microscopy 15.00 T 1-94 [» ]
2I2T X-ray 3.22 V 1-94 [» ]
2I2V X-ray 3.22 V 1-94 [» ]
2J28 electron microscopy 8.00 V 1-94 [» ]
2QAM X-ray 3.21 V 1-94 [» ]
2QAO X-ray 3.21 V 1-94 [» ]
2QBA X-ray 3.54 V 1-94 [» ]
2QBC X-ray 3.54 V 1-94 [» ]
2QBE X-ray 3.30 V 1-94 [» ]
2QBG X-ray 3.30 V 1-94 [» ]
2QBI X-ray 4.00 V 1-94 [» ]
2QBK X-ray 4.00 V 1-94 [» ]
2QOV X-ray 3.93 V 1-94 [» ]
2QOX X-ray 3.93 V 1-94 [» ]
2QOZ X-ray 3.50 V 1-94 [» ]
2QP1 X-ray 3.50 V 1-94 [» ]
2RDO electron microscopy 9.10 V 1-94 [» ]
2VHM X-ray 3.74 V 1-94 [» ]
2VHN X-ray 3.74 V 1-94 [» ]
2WWQ electron microscopy 5.80 W 1-94 [» ]
2Z4L X-ray 4.45 V 1-94 [» ]
2Z4N X-ray 4.45 V 1-94 [» ]
3BBX electron microscopy 10.00 V 1-94 [» ]
3DF2 X-ray 3.50 V 1-94 [» ]
3DF4 X-ray 3.50 V 1-94 [» ]
3E1B electron microscopy - C 1-94 [» ]
3E1D electron microscopy - C 1-94 [» ]
3FIK electron microscopy 6.70 V 1-94 [» ]
3I1N X-ray 3.19 V 1-94 [» ]
3I1P X-ray 3.19 V 1-94 [» ]
3I1R X-ray 3.81 V 1-94 [» ]
3I1T X-ray 3.81 V 1-94 [» ]
3I20 X-ray 3.71 V 1-94 [» ]
3I22 X-ray 3.71 V 1-94 [» ]
3IZT electron microscopy - W 1-94 [» ]
3IZU electron microscopy - W 1-94 [» ]
3J01 electron microscopy - V 1-94 [» ]
3J0T electron microscopy 12.10 X 1-94 [» ]
3J0W electron microscopy 14.70 X 1-94 [» ]
3J0Y electron microscopy 13.50 X 1-94 [» ]
3J11 electron microscopy 13.10 X 1-94 [» ]
3J12 electron microscopy 11.50 X 1-94 [» ]
3J14 electron microscopy 11.50 X 1-94 [» ]
3J19 electron microscopy 8.30 V 1-94 [» ]
3J37 electron microscopy 9.80 Z 1-94 [» ]
3J4X electron microscopy 12.00 V 1-94 [» ]
3J50 electron microscopy 20.00 V 1-94 [» ]
3J51 electron microscopy 17.00 V 1-94 [» ]
3J52 electron microscopy 12.00 V 1-94 [» ]
3J54 electron microscopy 13.00 V 1-94 [» ]
3J56 electron microscopy 15.00 V 1-94 [» ]
3J58 electron microscopy 17.00 V 1-94 [» ]
3J5A electron microscopy 12.00 V 1-94 [» ]
3J5C electron microscopy 17.00 V 1-94 [» ]
3J5E electron microscopy 17.00 V 1-94 [» ]
3J5G electron microscopy 20.00 V 1-94 [» ]
3J5I electron microscopy 15.00 V 1-94 [» ]
3J5K electron microscopy 9.00 V 1-94 [» ]
3J5L electron microscopy 6.60 V 1-94 [» ]
3J5O electron microscopy 6.80 V 1-94 [» ]
3J5U electron microscopy 7.60 X 1-94 [» ]
3J5W electron microscopy 7.60 Y 1-94 [» ]
3KCR electron microscopy - V 1-94 [» ]
3OAS X-ray 3.25 V 1-94 [» ]
3OAT X-ray 3.25 V 1-94 [» ]
3OFC X-ray 3.19 V 1-94 [» ]
3OFD X-ray 3.19 V 1-94 [» ]
3OFQ X-ray 3.10 V 1-94 [» ]
3OFR X-ray 3.10 V 1-94 [» ]
3OFZ X-ray 3.29 V 1-94 [» ]
3OG0 X-ray 3.29 V 1-94 [» ]
3ORB X-ray 3.30 V 1-94 [» ]
3R8S X-ray 3.00 V 1-94 [» ]
3R8T X-ray 3.00 V 1-94 [» ]
3SGF X-ray 3.20 Z 1-94 [» ]
3UOS X-ray 3.70 Z 1-94 [» ]
487D electron microscopy 7.50 N 1-94 [» ]
4CSU electron microscopy 5.50 W 1-94 [» ]
4GAR X-ray 3.30 V 1-94 [» ]
4GAU X-ray 3.30 V 1-94 [» ]
4KIX X-ray 2.90 V 1-94 [» ]
4KIZ X-ray 2.90 V 1-94 [» ]
4KJ1 X-ray 2.90 V 1-94 [» ]
4KJ3 X-ray 2.90 V 1-94 [» ]
4KJ5 X-ray 2.90 V 1-94 [» ]
4KJ7 X-ray 2.90 V 1-94 [» ]
4KJ9 X-ray 2.90 V 1-94 [» ]
4KJB X-ray 2.90 V 1-94 [» ]
ProteinModelPortali P68919.
SMRi P68919. Positions 1-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35885N.
IntActi P68919. 13 interactions.
MINTi MINT-1261165.
STRINGi 511145.b2185.

Chemistry

ChEMBLi CHEMBL2363135.

2D gel databases

SWISS-2DPAGE P68919.

Proteomic databases

PaxDbi P68919.
PRIDEi P68919.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75246 ; AAC75246 ; b2185 .
BAE76650 ; BAE76650 ; BAE76650 .
GeneIDi 12934501.
945618.
KEGGi ecj:Y75_p2148.
eco:b2185.
PATRICi 32119725. VBIEscCol129921_2273.

Organism-specific databases

EchoBASEi EB0878.
EcoGenei EG10885. rplY.

Phylogenomic databases

eggNOGi COG1825.
HOGENOMi HOG000277629.
KOi K02897.
OMAi SIELDHD.
OrthoDBi EOG6SZ1PC.
PhylomeDBi P68919.

Enzyme and pathway databases

BioCyci EcoCyc:EG10885-MONOMER.
ECOL316407:JW2173-MONOMER.

Miscellaneous databases

EvolutionaryTracei P68919.
PROi P68919.

Gene expression databases

Genevestigatori P68919.

Family and domain databases

Gene3Di 2.40.240.10. 1 hit.
HAMAPi MF_01336. Ribosomal_L25.
InterProi IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR020055. Ribosomal_L25_short.
[Graphical view ]
SUPFAMi SSF50715. SSF50715. 1 hit.
ProtoNeti Search...

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.

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: September 3, 2014
This is version 100 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

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