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Protein

50S ribosomal protein L11

Gene

rplK

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 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. The stalk extends beyond the surface of the 70S ribosome and is preferentially stabilized in 70S versus 50S crystals.
In the 70S ribosome is in a position where it could interact transiently with the A site tRNA during translation.

GO - Molecular functioni

  1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP
  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

BioCyciTTHE300852:GH8R-257-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L11UniRule annotation
Gene namesi
Name:rplKUniRule annotation
Ordered Locus Names:TTHA0247
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14714750S ribosomal protein L11PRO_0000104399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N6,N6,N6-trimethyllysine1 Publication

Post-translational modificationi

The protein probably contains twelve methyl groups; at least one lysine residue (Lys-3) is known to be trimethylated. Methylation of the protein is not required for function.2 Publications

Keywords - PTMi

Methylation

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 3 L12 dimers bind in a sequential fashion forming a heptameric L10(L12)2(L12)2(L12)2 complex. Contacts one of the L7 dimers.

Protein-protein interaction databases

IntActiQ5SLP6. 1 interaction.
MINTiMINT-4299414.
STRINGi300852.TTHA0247.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Turni20 – 223Combined sources
Helixi23 – 286Combined sources
Turni29 – 313Combined sources
Helixi34 – 4411Combined sources
Turni45 – 473Combined sources
Beta strandi52 – 609Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 695Combined sources
Helixi74 – 774Combined sources
Turni81 – 833Combined sources
Turni91 – 933Combined sources
Beta strandi97 – 993Combined sources
Helixi103 – 1108Combined sources
Turni111 – 1144Combined sources
Beta strandi118 – 1214Combined sources
Helixi123 – 1297Combined sources
Turni130 – 1356Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGVX-ray1.75B2-147[»]
4V42X-ray5.50L9-116[»]
4V4PX-ray5.50L6-116[»]
4V4TX-ray6.46K1-141[»]
4V4XX-ray5.00L1-147[»]
4V4YX-ray5.50L1-147[»]
4V4ZX-ray4.51L1-147[»]
4V51X-ray2.80K1-147[»]
4V5EX-ray3.45K1-147[»]
4V5FX-ray3.60K1-147[»]
4V5JX-ray3.10K1-147[»]
4V5Melectron microscopy7.80K1-147[»]
4V5Nelectron microscopy7.60K1-147[»]
4V68electron microscopy6.40L2-139[»]
4V6FX-ray3.10L1-147[»]
4V9HX-ray2.86K1-147[»]
4W2EX-ray2.90K1-147[»]
ProteinModelPortaliQ5SLP6.
SMRiQ5SLP6. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLP6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L11P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0080.
HOGENOMiHOG000082123.
KOiK02867.
OMAiKQFNAKT.
OrthoDBiEOG69PQ9D.
PhylomeDBiQ5SLP6.

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.

Q5SLP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVVAVVKL QLPAGKATPA PPVGPALGQH GANIMEFVKA FNAATANMGD
60 70 80 90 100
AIVPVEITIY ADRSFTFVTK TPPASYLIRK AAGLEKGAHK PGREKVGRIT
110 120 130 140
WEQVLEIAKQ KMPDLNTTDL EAAARMIAGS ARSMGVEVVG APEVKDA
Length:147
Mass (Da):15,505
Last modified:December 21, 2004 - v1
Checksum:i3D8DECEBE85B5FE9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201A → G AA sequence (PubMed:11154066).Curated
Sequence conflicti23 – 231V → G in L10348 (PubMed:1447157).Curated

Mass spectrometryi

Molecular mass is 15506.2 Da from positions 1 - 147. Determined by MALDI. Weight of the unmethylated protein.1 Publication
Molecular mass is 15675.1 Da from positions 1 - 147. Determined by MALDI. Weight of the methylated protein.1 Publication
Molecular mass is 15678 Da from positions 1 - 147. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70070.1.
L10348 Genomic DNA. No translation available.
RefSeqiWP_011174097.1. NC_006461.1.
YP_143513.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70070; BAD70070; BAD70070.
GeneIDi3168343.
KEGGittj:TTHA0247.
PATRICi23955441. VBITheThe93045_0247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70070.1.
L10348 Genomic DNA. No translation available.
RefSeqiWP_011174097.1. NC_006461.1.
YP_143513.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGVX-ray1.75B2-147[»]
4V42X-ray5.50L9-116[»]
4V4PX-ray5.50L6-116[»]
4V4TX-ray6.46K1-141[»]
4V4XX-ray5.00L1-147[»]
4V4YX-ray5.50L1-147[»]
4V4ZX-ray4.51L1-147[»]
4V51X-ray2.80K1-147[»]
4V5EX-ray3.45K1-147[»]
4V5FX-ray3.60K1-147[»]
4V5JX-ray3.10K1-147[»]
4V5Melectron microscopy7.80K1-147[»]
4V5Nelectron microscopy7.60K1-147[»]
4V68electron microscopy6.40L2-139[»]
4V6FX-ray3.10L1-147[»]
4V9HX-ray2.86K1-147[»]
4W2EX-ray2.90K1-147[»]
ProteinModelPortaliQ5SLP6.
SMRiQ5SLP6. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5SLP6. 1 interaction.
MINTiMINT-4299414.
STRINGi300852.TTHA0247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70070; BAD70070; BAD70070.
GeneIDi3168343.
KEGGittj:TTHA0247.
PATRICi23955441. VBITheThe93045_0247.

Phylogenomic databases

eggNOGiCOG0080.
HOGENOMiHOG000082123.
KOiK02867.
OMAiKQFNAKT.
OrthoDBiEOG69PQ9D.
PhylomeDBiQ5SLP6.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-257-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLP6.

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. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Identification of the gene encoding transcription factor NusG of Thermus thermophilus."
    Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.
    J. Bacteriol. 174:7859-7863(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
    Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
    Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-32 AND 71-85, BLOCKAGE OF N-TERMINUS.
  4. "Structural and functional studies on the overproduced L11 protein from Thermus thermophilus."
    Triantafillidou D., Simitsopoulou M., Franceschi F., Choli-Papadopoulou T.
    J. Protein Chem. 18:215-223(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-3.
  5. "Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for growth and preferentially modifies free ribosomal protein L11 prior to ribosome assembly."
    Cameron D.M., Gregory S.T., Thompson J., Suh M.-J., Limbach P.A., Dahlberg A.E.
    J. Bacteriol. 186:5819-5825(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, METHYLATION.
  6. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
    Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
    Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  7. "The path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL11_THET8
AccessioniPrimary (citable) accession number: Q5SLP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 88 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.