Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L11

Gene

rplK

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

Functioni

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.

GO - Molecular functioni

  1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP
  2. rRNA binding Source: EcoCyc
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. stringent response Source: EcoCyc
  2. translational termination Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10872-MONOMER.
ECOL316407:JW3946-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L11UniRule annotation
Gene namesi
Name:rplKUniRule annotation
Synonyms:relC
Ordered Locus Names:b3983, JW3946
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10872. rplK.

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
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 14214150S ribosomal protein L11PRO_0000104283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N,N-trimethylalanine1 Publication
Modified residuei4 – 41N6,N6,N6-trimethyllysine1 Publication
Modified residuei40 – 401N6,N6,N6-trimethyllysine1 Publication
Modified residuei72 – 721N6-succinyllysine1 Publication
Modified residuei81 – 811N6-succinyllysine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP0A7J7.
PRIDEiP0A7J7.

Expressioni

Gene expression databases

GenevestigatoriP0A7J7.

Interactioni

Subunit structurei

Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.

Binary interactionsi

WithEntry#Exp.IntActNotes
prmAP0A8T13EBI-547288,EBI-556300

Protein-protein interaction databases

BioGridi852778. 1 interaction.
DIPiDIP-35882N.
IntActiP0A7J7. 46 interactions.
MINTiMINT-1232893.
STRINGi511145.b3983.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Beta strandi9 – 135Combined sources
Beta strandi17 – 193Combined sources
Turni21 – 288Combined sources
Beta strandi29 – 324Combined sources
Beta strandi35 – 373Combined sources
Turni38 – 447Combined sources
Turni47 – 493Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 617Combined sources
Beta strandi63 – 653Combined sources
Beta strandi67 – 715Combined sources
Helixi78 – 803Combined sources
Beta strandi81 – 855Combined sources
Beta strandi87 – 893Combined sources
Turni93 – 953Combined sources
Beta strandi100 – 1045Combined sources
Helixi107 – 1115Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 1274Combined sources
Turni128 – 1336Combined sources
Helixi134 – 1363Combined sources
Beta strandi139 – 1413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50K1-140[»]
1MJ1electron microscopy13.00L1-141[»]
1ML5electron microscopy14.00l1-141[»]
2J28electron microscopy8.00I2-142[»]
2RDOelectron microscopy9.10I2-142[»]
3DEGelectron microscopy-H2-142[»]
3EP2electron microscopy-I2-142[»]
3EQ3electron microscopy-I2-142[»]
3EQ4electron microscopy-I2-142[»]
3J0Delectron microscopy11.10G2-142[»]
3J5Lelectron microscopy6.60I2-142[»]
3J7Zelectron microscopy3.90I1-142[»]
487Delectron microscopy7.50L10-86[»]
4CSUelectron microscopy5.50I2-142[»]
4U1UX-ray2.95BI/DI2-142[»]
4U1VX-ray3.00BI/DI2-142[»]
4U20X-ray2.90BI/DI2-142[»]
4U24X-ray2.90BI/DI2-142[»]
4U25X-ray2.90BI/DI2-142[»]
4U26X-ray2.80BI/DI2-142[»]
4U27X-ray2.80BI/DI2-142[»]
4V47electron microscopy12.30AG2-142[»]
4V48electron microscopy11.50AG2-142[»]
4V4HX-ray3.46BI/DI1-142[»]
4V4QX-ray3.46BI/DI2-142[»]
4V4Velectron microscopy15.00BG3-141[»]
4V4Welectron microscopy15.00BG3-141[»]
4V50X-ray3.22BI/DI2-142[»]
4V52X-ray3.21BI/DI2-142[»]
4V53X-ray3.54BI/DI2-142[»]
4V54X-ray3.30BI/DI2-142[»]
4V55X-ray4.00BI/DI2-142[»]
4V56X-ray3.93BI/DI2-142[»]
4V57X-ray3.50BI/DI2-142[»]
4V5BX-ray3.74AI/CI2-142[»]
4V5Helectron microscopy5.80BI2-142[»]
4V5YX-ray4.45BI/DI2-142[»]
4V64X-ray3.50BI/DI2-142[»]
4V65electron microscopy9.00B51-142[»]
4V66electron microscopy9.00B51-142[»]
4V69electron microscopy6.70BI2-142[»]
4V6CX-ray3.19BI/DI1-142[»]
4V6DX-ray3.81BI/DI1-142[»]
4V6EX-ray3.71BI/DI1-142[»]
4V6Kelectron microscopy8.25AJ1-142[»]
4V6Lelectron microscopy13.20BJ1-142[»]
4V6Melectron microscopy7.10BI2-142[»]
4V6Nelectron microscopy12.10AK2-142[»]
4V6Oelectron microscopy14.70BK2-142[»]
4V6Pelectron microscopy13.50BK2-142[»]
4V6Qelectron microscopy11.50BK2-142[»]
4V6Relectron microscopy11.50BK2-142[»]
4V6Selectron microscopy13.10AK2-142[»]
4V6Telectron microscopy8.30BI2-142[»]
4V6Velectron microscopy9.80K2-142[»]
4V6Yelectron microscopy12.00BI1-142[»]
4V6Zelectron microscopy12.00BI1-142[»]
4V70electron microscopy17.00BI1-142[»]
4V71electron microscopy20.00BI1-142[»]
4V72electron microscopy13.00BI1-142[»]
4V73electron microscopy15.00BI1-142[»]
4V74electron microscopy17.00BI1-142[»]
4V75electron microscopy12.00BI1-142[»]
4V76electron microscopy17.00BI1-142[»]
4V77electron microscopy17.00BI1-142[»]
4V78electron microscopy20.00BI1-142[»]
4V79electron microscopy15.00BI1-142[»]
4V7Aelectron microscopy9.00BI1-142[»]
4V7Belectron microscopy6.80BI1-142[»]
4V7Celectron microscopy7.60BK2-142[»]
4V7Delectron microscopy7.60AK2-142[»]
4V7Ielectron microscopy9.60AI1-142[»]
4V7SX-ray3.25BI/DI2-142[»]
4V7TX-ray3.19BI/DI2-142[»]
4V7UX-ray3.10BI/DI2-142[»]
4V7VX-ray3.29BI/DI2-142[»]
4V85X-ray3.20I1-142[»]
4V89X-ray3.70BI1-142[»]
4V9CX-ray3.30BI/DI1-142[»]
4V9DX-ray3.00CI/DI2-142[»]
4V9OX-ray2.90AI/CI/EI/GI1-142[»]
4V9PX-ray2.90AI/CI/EI/GI1-142[»]
4WF1X-ray3.09BI/DI2-142[»]
4WWWX-ray3.10RI/YI2-142[»]
ProteinModelPortaliP0A7J7.
SMRiP0A7J7. Positions 3-141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7J7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L11P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0080.
HOGENOMiHOG000082123.
InParanoidiP0A7J7.
KOiK02867.
OMAiKQFNAKT.
OrthoDBiEOG69PQ9D.
PhylomeDBiP0A7J7.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsiTIGR01632. L11_bact. 1 hit.
PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE
60 70 80 90 100
KGLPIPVVIT VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK
110 120 130 140
ISRAQLQEIA QTKAADMTGA DIEAMTRSIE GTARSMGLVV ED
Length:142
Mass (Da):14,875
Last modified:January 23, 2007 - v2
Checksum:iC49226BB2462BE0F
GO

Mass spectrometryi

Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.
PIRiS12572. R5EC11.
RefSeqiNP_418410.1. NC_000913.3.
YP_491478.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76957; AAC76957; b3983.
BAE77337; BAE77337; BAE77337.
GeneIDi12930523.
948484.
KEGGiecj:Y75_p3214.
eco:b3983.
PATRICi32123487. VBIEscCol129921_4096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.
PIRiS12572. R5EC11.
RefSeqiNP_418410.1. NC_000913.3.
YP_491478.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50K1-140[»]
1MJ1electron microscopy13.00L1-141[»]
1ML5electron microscopy14.00l1-141[»]
2J28electron microscopy8.00I2-142[»]
2RDOelectron microscopy9.10I2-142[»]
3DEGelectron microscopy-H2-142[»]
3EP2electron microscopy-I2-142[»]
3EQ3electron microscopy-I2-142[»]
3EQ4electron microscopy-I2-142[»]
3J0Delectron microscopy11.10G2-142[»]
3J5Lelectron microscopy6.60I2-142[»]
3J7Zelectron microscopy3.90I1-142[»]
487Delectron microscopy7.50L10-86[»]
4CSUelectron microscopy5.50I2-142[»]
4U1UX-ray2.95BI/DI2-142[»]
4U1VX-ray3.00BI/DI2-142[»]
4U20X-ray2.90BI/DI2-142[»]
4U24X-ray2.90BI/DI2-142[»]
4U25X-ray2.90BI/DI2-142[»]
4U26X-ray2.80BI/DI2-142[»]
4U27X-ray2.80BI/DI2-142[»]
4V47electron microscopy12.30AG2-142[»]
4V48electron microscopy11.50AG2-142[»]
4V4HX-ray3.46BI/DI1-142[»]
4V4QX-ray3.46BI/DI2-142[»]
4V4Velectron microscopy15.00BG3-141[»]
4V4Welectron microscopy15.00BG3-141[»]
4V50X-ray3.22BI/DI2-142[»]
4V52X-ray3.21BI/DI2-142[»]
4V53X-ray3.54BI/DI2-142[»]
4V54X-ray3.30BI/DI2-142[»]
4V55X-ray4.00BI/DI2-142[»]
4V56X-ray3.93BI/DI2-142[»]
4V57X-ray3.50BI/DI2-142[»]
4V5BX-ray3.74AI/CI2-142[»]
4V5Helectron microscopy5.80BI2-142[»]
4V5YX-ray4.45BI/DI2-142[»]
4V64X-ray3.50BI/DI2-142[»]
4V65electron microscopy9.00B51-142[»]
4V66electron microscopy9.00B51-142[»]
4V69electron microscopy6.70BI2-142[»]
4V6CX-ray3.19BI/DI1-142[»]
4V6DX-ray3.81BI/DI1-142[»]
4V6EX-ray3.71BI/DI1-142[»]
4V6Kelectron microscopy8.25AJ1-142[»]
4V6Lelectron microscopy13.20BJ1-142[»]
4V6Melectron microscopy7.10BI2-142[»]
4V6Nelectron microscopy12.10AK2-142[»]
4V6Oelectron microscopy14.70BK2-142[»]
4V6Pelectron microscopy13.50BK2-142[»]
4V6Qelectron microscopy11.50BK2-142[»]
4V6Relectron microscopy11.50BK2-142[»]
4V6Selectron microscopy13.10AK2-142[»]
4V6Telectron microscopy8.30BI2-142[»]
4V6Velectron microscopy9.80K2-142[»]
4V6Yelectron microscopy12.00BI1-142[»]
4V6Zelectron microscopy12.00BI1-142[»]
4V70electron microscopy17.00BI1-142[»]
4V71electron microscopy20.00BI1-142[»]
4V72electron microscopy13.00BI1-142[»]
4V73electron microscopy15.00BI1-142[»]
4V74electron microscopy17.00BI1-142[»]
4V75electron microscopy12.00BI1-142[»]
4V76electron microscopy17.00BI1-142[»]
4V77electron microscopy17.00BI1-142[»]
4V78electron microscopy20.00BI1-142[»]
4V79electron microscopy15.00BI1-142[»]
4V7Aelectron microscopy9.00BI1-142[»]
4V7Belectron microscopy6.80BI1-142[»]
4V7Celectron microscopy7.60BK2-142[»]
4V7Delectron microscopy7.60AK2-142[»]
4V7Ielectron microscopy9.60AI1-142[»]
4V7SX-ray3.25BI/DI2-142[»]
4V7TX-ray3.19BI/DI2-142[»]
4V7UX-ray3.10BI/DI2-142[»]
4V7VX-ray3.29BI/DI2-142[»]
4V85X-ray3.20I1-142[»]
4V89X-ray3.70BI1-142[»]
4V9CX-ray3.30BI/DI1-142[»]
4V9DX-ray3.00CI/DI2-142[»]
4V9OX-ray2.90AI/CI/EI/GI1-142[»]
4V9PX-ray2.90AI/CI/EI/GI1-142[»]
4WF1X-ray3.09BI/DI2-142[»]
4WWWX-ray3.10RI/YI2-142[»]
ProteinModelPortaliP0A7J7.
SMRiP0A7J7. Positions 3-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852778. 1 interaction.
DIPiDIP-35882N.
IntActiP0A7J7. 46 interactions.
MINTiMINT-1232893.
STRINGi511145.b3983.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7J7.
PRIDEiP0A7J7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76957; AAC76957; b3983.
BAE77337; BAE77337; BAE77337.
GeneIDi12930523.
948484.
KEGGiecj:Y75_p3214.
eco:b3983.
PATRICi32123487. VBIEscCol129921_4096.

Organism-specific databases

EchoBASEiEB0865.
EcoGeneiEG10872. rplK.

Phylogenomic databases

eggNOGiCOG0080.
HOGENOMiHOG000082123.
InParanoidiP0A7J7.
KOiK02867.
OMAiKQFNAKT.
OrthoDBiEOG69PQ9D.
PhylomeDBiP0A7J7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10872-MONOMER.
ECOL316407:JW3946-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7J7.
PROiP0A7J7.

Gene expression databases

GenevestigatoriP0A7J7.

Family and domain databases

Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11.
InterProiIPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTiSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsiTIGR01632. L11_bact. 1 hit.
PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
    Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
    Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes."
    Dognin M.J., Wittmann-Liebold B.
    Eur. J. Biochem. 112:131-151(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-142, METHYLATION AT ALA-2; LYS-4 AND LYS-40.
    Strain: K12.
  6. "Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
    Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
    J. Bacteriol. 172:1621-1627(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
  7. "Structural properties of ribosomal protein L11 from Escherichia coli."
    Choli T.
    Biochem. Int. 19:1323-1338(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURAL STUDIES.
  8. "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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  10. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  11. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-72 AND LYS-81.
    Strain: K12.
  12. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL11_ECOLI
AccessioniPrimary (citable) accession number: P0A7J7
Secondary accession number(s): P02409, P76778, Q2M8R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 105 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.