SubmitCancel

Skip Header

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

Q5SLP6

- RL11_THET8

UniProt

Q5SLP6 - RL11_THET8

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
50S ribosomal protein L11
Gene
rplK, TTHA0247
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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.UniRule annotation
In the 70S ribosome is in a position where it could interact transiently with the A site tRNA during translation.UniRule annotation

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 L11
Gene namesi
Name:rplK
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 L11UniRule annotation
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50L9-116[»]
1YL3X-ray5.50L6-116[»]
2B9PX-ray6.46K1-141[»]
2HGJX-ray5.00L1-147[»]
2HGQX-ray5.50L1-147[»]
2HGUX-ray4.51L1-147[»]
2J01X-ray2.80K1-147[»]
2J03X-ray2.80K1-147[»]
2WH2X-ray3.45K1-147[»]
2WH4X-ray3.45K1-147[»]
2WRJX-ray3.60K1-147[»]
2WRLX-ray3.60K1-147[»]
2X9SX-ray3.10K1-147[»]
2X9UX-ray3.10K1-147[»]
2XTGelectron microscopy7.80K1-147[»]
2XUXelectron microscopy7.60K1-147[»]
3EGVX-ray1.75B2-147[»]
3FINelectron microscopy6.40L2-139[»]
3I8IX-ray3.10L1-147[»]
4JUXX-ray2.86K1-147[»]
ProteinModelPortaliQ5SLP6.
SMRiQ5SLP6. Positions 1-147.

Miscellaneous databases

EvolutionaryTraceiQ5SLP6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0080.
HOGENOMiHOG000082123.
KOiK02867.
OMAiIEAYIKL.
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

MKKVVAVVKL QLPAGKATPA PPVGPALGQH GANIMEFVKA FNAATANMGD    50
AIVPVEITIY ADRSFTFVTK TPPASYLIRK AAGLEKGAHK PGREKVGRIT 100
WEQVLEIAKQ KMPDLNTTDL EAAARMIAGS ARSMGVEVVG APEVKDA 147
Length:147
Mass (Da):15,505
Last modified:December 21, 2004 - v1
Checksum:i3D8DECEBE85B5FE9
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201A → G AA sequence 1 Publication
Sequence conflicti23 – 231V → G in L10348. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70070.1.
L10348 Genomic DNA. No translation available.
RefSeqiYP_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:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70070.1 .
L10348 Genomic DNA. No translation available.
RefSeqi YP_143513.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GIY X-ray 5.50 L 9-116 [» ]
1YL3 X-ray 5.50 L 6-116 [» ]
2B9P X-ray 6.46 K 1-141 [» ]
2HGJ X-ray 5.00 L 1-147 [» ]
2HGQ X-ray 5.50 L 1-147 [» ]
2HGU X-ray 4.51 L 1-147 [» ]
2J01 X-ray 2.80 K 1-147 [» ]
2J03 X-ray 2.80 K 1-147 [» ]
2WH2 X-ray 3.45 K 1-147 [» ]
2WH4 X-ray 3.45 K 1-147 [» ]
2WRJ X-ray 3.60 K 1-147 [» ]
2WRL X-ray 3.60 K 1-147 [» ]
2X9S X-ray 3.10 K 1-147 [» ]
2X9U X-ray 3.10 K 1-147 [» ]
2XTG electron microscopy 7.80 K 1-147 [» ]
2XUX electron microscopy 7.60 K 1-147 [» ]
3EGV X-ray 1.75 B 2-147 [» ]
3FIN electron microscopy 6.40 L 2-139 [» ]
3I8I X-ray 3.10 L 1-147 [» ]
4JUX X-ray 2.86 K 1-147 [» ]
ProteinModelPortali Q5SLP6.
SMRi Q5SLP6. Positions 1-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q5SLP6. 1 interaction.
MINTi MINT-4299414.
STRINGi 300852.TTHA0247.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70070 ; BAD70070 ; BAD70070 .
GeneIDi 3168343.
KEGGi ttj:TTHA0247.
PATRICi 23955441. VBITheThe93045_0247.

Phylogenomic databases

eggNOGi COG0080.
HOGENOMi HOG000082123.
KOi K02867.
OMAi IEAYIKL.
OrthoDBi EOG69PQ9D.
PhylomeDBi Q5SLP6.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-257-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SLP6.

Family and domain databases

Gene3Di 1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPi MF_00736. Ribosomal_L11.
InterProi IPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view ]
PANTHERi PTHR11661. PTHR11661. 1 hit.
Pfami PF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view ]
SMARTi SM00649. RL11. 1 hit.
[Graphical view ]
SUPFAMi SSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsi TIGR01632. L11_bact. 1 hit.
PROSITEi PS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 82 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