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Protein

50S ribosomal protein L6

Gene

rplF

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

Functioni

This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.1 Publication
Gentamicin-resistant mutations in this protein affect translation fidelity.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10869-MONOMER.
ECOL316407:JW3267-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L6UniRule annotation
Gene namesi
Name:rplFUniRule annotation
Ordered Locus Names:b3305, JW3267
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10869. rplF.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 17717650S ribosomal protein L6PRO_0000131048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysineUniRule annotation1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AG55.
PRIDEiP0AG55.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

BioGridi852115. 1 interaction.
DIPiDIP-35860N.
IntActiP0AG55. 83 interactions.
MINTiMINT-1244940.
STRINGi511145.b3305.

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Beta strandi18 – 203Combined sources
Beta strandi23 – 286Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 468Combined sources
Beta strandi49 – 546Combined sources
Beta strandi55 – 573Combined sources
Helixi61 – 7818Combined sources
Turni79 – 813Combined sources
Beta strandi83 – 886Combined sources
Beta strandi89 – 913Combined sources
Beta strandi95 – 995Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi122 – 1276Combined sources
Beta strandi130 – 1367Combined sources
Helixi138 – 15013Combined sources
Turni156 – 1583Combined sources
Beta strandi163 – 1664Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50J1-171[»]
1ML5electron microscopy14.00h2-177[»]
2J28electron microscopy8.00G2-177[»]
2RDOelectron microscopy9.10G2-177[»]
3BBXelectron microscopy10.00G2-177[»]
3J5Lelectron microscopy6.60G2-177[»]
3J7Zelectron microscopy3.90G1-177[»]
3J9Yelectron microscopy3.90G1-177[»]
487Delectron microscopy7.50J31-165[»]
4CSUelectron microscopy5.50G2-177[»]
4U1UX-ray2.95BG/DG2-177[»]
4U1VX-ray3.00BG/DG2-177[»]
4U20X-ray2.90BG/DG2-177[»]
4U24X-ray2.90BG/DG2-177[»]
4U25X-ray2.90BG/DG2-177[»]
4U26X-ray2.80BG/DG2-177[»]
4U27X-ray2.80BG/DG2-177[»]
4UY8electron microscopy3.80G2-177[»]
4V47electron microscopy12.30AE2-177[»]
4V48electron microscopy11.50AE2-177[»]
4V4HX-ray3.46BG/DG1-177[»]
4V4QX-ray3.46BG/DG2-177[»]
4V4Velectron microscopy15.00BE6-172[»]
4V4Welectron microscopy15.00BE6-172[»]
4V50X-ray3.22BG/DG2-177[»]
4V52X-ray3.21BG/DG2-177[»]
4V53X-ray3.54BG/DG2-177[»]
4V54X-ray3.30BG/DG2-177[»]
4V55X-ray4.00BG/DG2-177[»]
4V56X-ray3.93BG/DG2-177[»]
4V57X-ray3.50BG/DG2-177[»]
4V5BX-ray3.74AG/CG2-177[»]
4V5Helectron microscopy5.80BG2-177[»]
4V5YX-ray4.45BG/DG2-177[»]
4V64X-ray3.50BG/DG2-177[»]
4V65electron microscopy9.00B31-177[»]
4V66electron microscopy9.00B31-177[»]
4V69electron microscopy6.70BG2-177[»]
4V6CX-ray3.19BG/DG1-177[»]
4V6DX-ray3.81BG/DG1-177[»]
4V6EX-ray3.71BG/DG1-177[»]
4V6Kelectron microscopy8.25AH1-177[»]
4V6Lelectron microscopy13.20BH1-177[»]
4V6Melectron microscopy7.10BG2-177[»]
4V6Nelectron microscopy12.10AH2-177[»]
4V6Oelectron microscopy14.70BH2-177[»]
4V6Pelectron microscopy13.50BH2-177[»]
4V6Qelectron microscopy11.50BH2-177[»]
4V6Relectron microscopy11.50BH2-177[»]
4V6Selectron microscopy13.10AH2-177[»]
4V6Telectron microscopy8.30BG2-177[»]
4V6Velectron microscopy9.80BH2-177[»]
4V6Yelectron microscopy12.00BG1-177[»]
4V6Zelectron microscopy12.00BG1-177[»]
4V70electron microscopy17.00BG1-177[»]
4V71electron microscopy20.00BG1-177[»]
4V72electron microscopy13.00BG1-177[»]
4V73electron microscopy15.00BG1-177[»]
4V74electron microscopy17.00BG1-177[»]
4V75electron microscopy12.00BG1-177[»]
4V76electron microscopy17.00BG1-177[»]
4V77electron microscopy17.00BG1-177[»]
4V78electron microscopy20.00BG1-177[»]
4V79electron microscopy15.00BG1-177[»]
4V7Aelectron microscopy9.00BG1-177[»]
4V7Belectron microscopy6.80BG1-177[»]
4V7Celectron microscopy7.60BH2-177[»]
4V7Delectron microscopy7.60AH2-177[»]
4V7Ielectron microscopy9.60AG1-177[»]
4V7SX-ray3.25BG/DG2-177[»]
4V7TX-ray3.19BG/DG2-177[»]
4V7UX-ray3.10BG/DG2-177[»]
4V7VX-ray3.29BG/DG2-177[»]
4V85X-ray3.20G1-177[»]
4V89X-ray3.70BG1-177[»]
4V9CX-ray3.30BG/DG1-177[»]
4V9DX-ray3.00CG/DG2-177[»]
4V9OX-ray2.90AG/CG/EG/GG1-177[»]
4V9PX-ray2.90AG/CG/EG/GG1-177[»]
4WF1X-ray3.09BG/DG2-177[»]
4WWWX-ray3.10RG/YG2-177[»]
4YBBX-ray2.10CG/DG2-177[»]
5AFIelectron microscopy2.90G1-177[»]
5AKAelectron microscopy5.70G2-177[»]
ProteinModelPortaliP0AG55.
SMRiP0AG55. Positions 2-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG55.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L6P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039903.
InParanoidiP0AG55.
KOiK02933.
OMAiMPAGITV.
OrthoDBiEOG67DPRD.
PhylomeDBiP0AG55.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
HAMAPiMF_01365_B. Ribosomal_L6_B.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR019906. Ribosomal_L6_bac-type.
IPR002358. Ribosomal_L6_CS.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
PRINTSiPR00059. RIBOSOMALL6.
SUPFAMiSSF56053. SSF56053. 2 hits.
TIGRFAMsiTIGR03654. L6_bact. 1 hit.
PROSITEiPS00525. RIBOSOMAL_L6_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AG55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVAKAPVV VPAGVDVKIN GQVITIKGKN GELTRTLNDA VEVKHADNTL
60 70 80 90 100
TFGPRDGYAD GWAQAGTARA LLNSMVIGVT EGFTKKLQLV GVGYRAAVKG
110 120 130 140 150
NVINLSLGFS HPVDHQLPAG ITAECPTQTE IVLKGADKQV IGQVAADLRA
160 170
YRRPEPYKGK GVRYADEVVR TKEAKKK
Length:177
Mass (Da):18,904
Last modified:January 23, 2007 - v2
Checksum:i946B64E9FA42FE61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821G → D in CAA25720 (PubMed:6222285).Curated
Sequence conflicti88 – 881Q → E AA sequence (PubMed:324885).Curated

Mass spectrometryi

Molecular mass is 18772.7 Da from positions 2 - 177. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 17726RRPEP…EAKKK → AL in gentamicin resistant strain: GS50-15. 1 Publication
Add
BLAST
Natural varianti158 – 17720KGKGV…EAKKK → TL in gentamicin resistant strain: GS20-8. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25720.1.
U18997 Genomic DNA. Translation: AAA58102.1.
U00096 Genomic DNA. Translation: AAC76330.1.
AP009048 Genomic DNA. Translation: BAE77986.1.
PIRiD65123. R5EC6.
RefSeqiNP_417764.1. NC_000913.3.
WP_000091945.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76330; AAC76330; b3305.
BAE77986; BAE77986; BAE77986.
GeneIDi947803.
KEGGieco:b3305.
PATRICi32122042. VBIEscCol129921_3398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25720.1.
U18997 Genomic DNA. Translation: AAA58102.1.
U00096 Genomic DNA. Translation: AAC76330.1.
AP009048 Genomic DNA. Translation: BAE77986.1.
PIRiD65123. R5EC6.
RefSeqiNP_417764.1. NC_000913.3.
WP_000091945.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50J1-171[»]
1ML5electron microscopy14.00h2-177[»]
2J28electron microscopy8.00G2-177[»]
2RDOelectron microscopy9.10G2-177[»]
3BBXelectron microscopy10.00G2-177[»]
3J5Lelectron microscopy6.60G2-177[»]
3J7Zelectron microscopy3.90G1-177[»]
3J9Yelectron microscopy3.90G1-177[»]
487Delectron microscopy7.50J31-165[»]
4CSUelectron microscopy5.50G2-177[»]
4U1UX-ray2.95BG/DG2-177[»]
4U1VX-ray3.00BG/DG2-177[»]
4U20X-ray2.90BG/DG2-177[»]
4U24X-ray2.90BG/DG2-177[»]
4U25X-ray2.90BG/DG2-177[»]
4U26X-ray2.80BG/DG2-177[»]
4U27X-ray2.80BG/DG2-177[»]
4UY8electron microscopy3.80G2-177[»]
4V47electron microscopy12.30AE2-177[»]
4V48electron microscopy11.50AE2-177[»]
4V4HX-ray3.46BG/DG1-177[»]
4V4QX-ray3.46BG/DG2-177[»]
4V4Velectron microscopy15.00BE6-172[»]
4V4Welectron microscopy15.00BE6-172[»]
4V50X-ray3.22BG/DG2-177[»]
4V52X-ray3.21BG/DG2-177[»]
4V53X-ray3.54BG/DG2-177[»]
4V54X-ray3.30BG/DG2-177[»]
4V55X-ray4.00BG/DG2-177[»]
4V56X-ray3.93BG/DG2-177[»]
4V57X-ray3.50BG/DG2-177[»]
4V5BX-ray3.74AG/CG2-177[»]
4V5Helectron microscopy5.80BG2-177[»]
4V5YX-ray4.45BG/DG2-177[»]
4V64X-ray3.50BG/DG2-177[»]
4V65electron microscopy9.00B31-177[»]
4V66electron microscopy9.00B31-177[»]
4V69electron microscopy6.70BG2-177[»]
4V6CX-ray3.19BG/DG1-177[»]
4V6DX-ray3.81BG/DG1-177[»]
4V6EX-ray3.71BG/DG1-177[»]
4V6Kelectron microscopy8.25AH1-177[»]
4V6Lelectron microscopy13.20BH1-177[»]
4V6Melectron microscopy7.10BG2-177[»]
4V6Nelectron microscopy12.10AH2-177[»]
4V6Oelectron microscopy14.70BH2-177[»]
4V6Pelectron microscopy13.50BH2-177[»]
4V6Qelectron microscopy11.50BH2-177[»]
4V6Relectron microscopy11.50BH2-177[»]
4V6Selectron microscopy13.10AH2-177[»]
4V6Telectron microscopy8.30BG2-177[»]
4V6Velectron microscopy9.80BH2-177[»]
4V6Yelectron microscopy12.00BG1-177[»]
4V6Zelectron microscopy12.00BG1-177[»]
4V70electron microscopy17.00BG1-177[»]
4V71electron microscopy20.00BG1-177[»]
4V72electron microscopy13.00BG1-177[»]
4V73electron microscopy15.00BG1-177[»]
4V74electron microscopy17.00BG1-177[»]
4V75electron microscopy12.00BG1-177[»]
4V76electron microscopy17.00BG1-177[»]
4V77electron microscopy17.00BG1-177[»]
4V78electron microscopy20.00BG1-177[»]
4V79electron microscopy15.00BG1-177[»]
4V7Aelectron microscopy9.00BG1-177[»]
4V7Belectron microscopy6.80BG1-177[»]
4V7Celectron microscopy7.60BH2-177[»]
4V7Delectron microscopy7.60AH2-177[»]
4V7Ielectron microscopy9.60AG1-177[»]
4V7SX-ray3.25BG/DG2-177[»]
4V7TX-ray3.19BG/DG2-177[»]
4V7UX-ray3.10BG/DG2-177[»]
4V7VX-ray3.29BG/DG2-177[»]
4V85X-ray3.20G1-177[»]
4V89X-ray3.70BG1-177[»]
4V9CX-ray3.30BG/DG1-177[»]
4V9DX-ray3.00CG/DG2-177[»]
4V9OX-ray2.90AG/CG/EG/GG1-177[»]
4V9PX-ray2.90AG/CG/EG/GG1-177[»]
4WF1X-ray3.09BG/DG2-177[»]
4WWWX-ray3.10RG/YG2-177[»]
4YBBX-ray2.10CG/DG2-177[»]
5AFIelectron microscopy2.90G1-177[»]
5AKAelectron microscopy5.70G2-177[»]
ProteinModelPortaliP0AG55.
SMRiP0AG55. Positions 2-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852115. 1 interaction.
DIPiDIP-35860N.
IntActiP0AG55. 83 interactions.
MINTiMINT-1244940.
STRINGi511145.b3305.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0AG55.
PRIDEiP0AG55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76330; AAC76330; b3305.
BAE77986; BAE77986; BAE77986.
GeneIDi947803.
KEGGieco:b3305.
PATRICi32122042. VBIEscCol129921_3398.

Organism-specific databases

EchoBASEiEB0862.
EcoGeneiEG10869. rplF.

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039903.
InParanoidiP0AG55.
KOiK02933.
OMAiMPAGITV.
OrthoDBiEOG67DPRD.
PhylomeDBiP0AG55.

Enzyme and pathway databases

BioCyciEcoCyc:EG10869-MONOMER.
ECOL316407:JW3267-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG55.
PROiP0AG55.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
HAMAPiMF_01365_B. Ribosomal_L6_B.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR019906. Ribosomal_L6_bac-type.
IPR002358. Ribosomal_L6_CS.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
PRINTSiPR00059. RIBOSOMALL6.
SUPFAMiSSF56053. SSF56053. 2 hits.
TIGRFAMsiTIGR03654. L6_bact. 1 hit.
PROSITEiPS00525. RIBOSOMAL_L6_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein L6 from the aminoacyl-tRNA binding site of the Escherichia coli ribosome."
    Chen R., Arfsten U., Chen-Schmeisser U.
    Hoppe-Seyler's Z. Physiol. Chem. 358:531-535(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-177.
    Strain: K.
  2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "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 2-13.
    Strain: K12 / EMG2.
  6. "Alteration of ribosomal protein L6 in gentamicin-resistant strains of Escherichia coli. Effects on fidelity of protein synthesis."
    Kuehberger R., Piepersberg W., Petzet A., Buckel P., Boeck A.
    Biochemistry 18:187-193(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOLATION, CHARACTERIZATION OF VARIANTS GENTAMICIN-RESISTANT GE20-8; GS20-10 AND GS50-15.
    Strain: K12 / A19.
  7. "The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
    Wower I., Wower J., Meinke M., Brimacombe R.
    Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO 23S RRNA.
    Strain: MRE-600.
  8. "Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance."
    Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., White S.W.
    J. Mol. Biol. 279:873-888(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF VARIANTS GENTAMICIN-RESISTANT.
  9. "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.
  10. "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.
  11. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  12. "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.
  13. "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.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  15. "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 2-177 IN TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL6_ECOLI
AccessioniPrimary (citable) accession number: P0AG55
Secondary accession number(s): P02390, Q2M6X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 100 of the entry and version 2 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.