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Protein

50S ribosomal protein L18

Gene

rplR

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

This is one of the proteins that binds and mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1715-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L18
Alternative name(s):
TL24
Gene namesi
Name:rplR
Ordered Locus Names:TTHA1676
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 11211150S ribosomal protein L18PRO_0000131372Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and probably the 23S rRNA; has been isolated in a complex with the 5S rRNA and RL25 (Ref. 2).

Protein-protein interaction databases

STRINGi300852.TTHA1676.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 194Combined sources
Beta strandi25 – 306Combined sources
Beta strandi35 – 417Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 516Combined sources
Helixi54 – 563Combined sources
Helixi63 – 7917Combined sources
Beta strandi102 – 1043Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RS/YS1-112[»]
1VY4X-ray2.60BS/DS1-112[»]
1VY5X-ray2.55BS/DS1-112[»]
1VY6X-ray2.90BS/DS1-112[»]
1VY7X-ray2.80BS/DS1-112[»]
4L47X-ray3.22RS/YS1-112[»]
4L71X-ray3.90RS/YS1-112[»]
4LELX-ray3.90RS/YS1-112[»]
4LFZX-ray3.92RS/YS1-112[»]
4LNTX-ray2.94RS/YS1-112[»]
4LSKX-ray3.48RS/YS1-112[»]
4LT8X-ray3.14RS/YS1-112[»]
4P6FX-ray3.60RS/YS1-112[»]
4P70X-ray3.68RS/YS1-112[»]
4TUAX-ray3.60RS/YS1-112[»]
4TUBX-ray3.60RS/YS1-112[»]
4TUCX-ray3.60RS/YS1-112[»]
4TUDX-ray3.60RS/YS1-112[»]
4TUEX-ray3.50RS/YS1-112[»]
4V42X-ray5.50BQ1-112[»]
4V4PX-ray5.50Q1-112[»]
4V4XX-ray5.00BR1-112[»]
4V4YX-ray5.50BR1-112[»]
4V4ZX-ray4.51BR1-112[»]
4V51X-ray2.80BS/DS2-112[»]
4V5AX-ray3.50BS/DS2-112[»]
4V5CX-ray3.30BS/DS1-112[»]
4V5DX-ray3.50BS/DS1-112[»]
4V5EX-ray3.45BS/DS1-112[»]
4V5FX-ray3.60BS/DS1-112[»]
4V5GX-ray3.60BS/DS1-112[»]
4V5JX-ray3.10BS/DS1-112[»]
4V5KX-ray3.20BS/DS1-112[»]
4V5LX-ray3.10BS1-112[»]
4V5Melectron microscopy7.80BS1-112[»]
4V5Nelectron microscopy7.60BS1-112[»]
4V5PX-ray3.10BS/DS1-112[»]
4V5QX-ray3.10BS/DS1-112[»]
4V5RX-ray3.10BS/DS1-112[»]
4V5SX-ray3.10BS/DS1-112[»]
4V68electron microscopy6.40BS11-109[»]
4V6AX-ray3.10BS/DS1-112[»]
4V6FX-ray3.10AQ/DQ1-112[»]
4V6GX-ray3.50BQ/DQ1-112[»]
4V7JX-ray3.30AS/BS1-112[»]
4V7KX-ray3.60AS/BS1-112[»]
4V7LX-ray3.00BS/DS1-112[»]
4V7MX-ray3.45BS/DS1-112[»]
4V7WX-ray3.00BS/DS1-112[»]
4V7XX-ray3.00BS/DS1-112[»]
4V7YX-ray3.00BS/DS1-112[»]
4V7ZX-ray3.10BS/DS1-112[»]
4V87X-ray3.10AQ/DQ2-112[»]
4V8AX-ray3.20AS/BS1-112[»]
4V8BX-ray3.00BQ/DQ1-112[»]
4V8CX-ray3.30AQ/BQ1-112[»]
4V8DX-ray3.00BQ/DQ1-112[»]
4V8EX-ray3.30AQ/CQ1-112[»]
4V8FX-ray3.30AQ/DQ1-112[»]
4V8GX-ray3.00BS/DS1-112[»]
4V8HX-ray3.10BS/DS1-112[»]
4V8IX-ray2.70BS/DS1-112[»]
4V8JX-ray3.90BS/DS1-112[»]
4V8NX-ray3.10BS/DS1-112[»]
4V8OX-ray3.80BS1-112[»]
4V8QX-ray3.10AS1-112[»]
4V8UX-ray3.70BS/DS1-112[»]
4V8XX-ray3.35BS/DS1-112[»]
4V90X-ray2.95BS2-112[»]
4V95X-ray3.20BS/DS1-112[»]
4V97X-ray3.52BS/DS1-112[»]
4V9AX-ray3.30BQ/DQ1-112[»]
4V9BX-ray3.10BQ/DQ1-112[»]
4V9HX-ray2.86BS1-112[»]
4V9IX-ray3.30BS/DS11-108[»]
4V9RX-ray3.00BS/DS1-112[»]
4V9SX-ray3.10BS/DS1-112[»]
4W2EX-ray2.90S1-112[»]
4W2FX-ray2.40BS/DS1-112[»]
4W2GX-ray2.55BS/DS1-112[»]
4W2HX-ray2.70BS/DS1-112[»]
4W2IX-ray2.70BS/DS1-112[»]
4WPOX-ray2.80AS/CS1-112[»]
4WQFX-ray2.80AS/CS1-112[»]
4WQUX-ray2.80AS/CS1-112[»]
4WQYX-ray2.80AS/CS1-112[»]
4WWEX-ray3.40R11-108[»]
4WWTX-ray3.40R11-108[»]
4Y4OX-ray2.301S/2S1-112[»]
4Y4PX-ray2.501S/2S1-112[»]
ProteinModelPortaliQ5SHQ4.
SMRiQ5SHQ4. Positions 3-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHQ4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

eggNOGiCOG0256.
HOGENOMiHOG000248742.
KOiK02881.
OMAiSYRYHGR.
OrthoDBiEOG64NB48.
PhylomeDBiQ5SHQ4.

Family and domain databases

HAMAPiMF_01337_B. Ribosomal_L18_B.
InterProiIPR005484. Ribosomal_L18/L5.
IPR004389. Ribosomal_L18_bac-type.
[Graphical view]
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00060. L18_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5SHQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLTAYERR KFRVRNRIKR TGRLRLSVFR SLKHIYAQII DDEKGVTLVS
60 70 80 90 100
ASSLALKLKG NKTEVARQVG RALAEKALAL GIKQVAFDRG PYKYHGRVKA
110
LAEGAREGGL EF
Length:112
Mass (Da):12,612
Last modified:January 23, 2007 - v3
Checksum:iEA2AB016AEDB0638
GO

Mass spectrometryi

Molecular mass is 12481 Da from positions 2 - 112. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71499.1.
RefSeqiWP_008633391.1. NC_006461.1.
YP_144942.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71499; BAD71499; BAD71499.
GeneIDi3169978.
KEGGittj:TTHA1676.
PATRICi23958307. VBITheThe93045_1646.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71499.1.
RefSeqiWP_008633391.1. NC_006461.1.
YP_144942.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RS/YS1-112[»]
1VY4X-ray2.60BS/DS1-112[»]
1VY5X-ray2.55BS/DS1-112[»]
1VY6X-ray2.90BS/DS1-112[»]
1VY7X-ray2.80BS/DS1-112[»]
4L47X-ray3.22RS/YS1-112[»]
4L71X-ray3.90RS/YS1-112[»]
4LELX-ray3.90RS/YS1-112[»]
4LFZX-ray3.92RS/YS1-112[»]
4LNTX-ray2.94RS/YS1-112[»]
4LSKX-ray3.48RS/YS1-112[»]
4LT8X-ray3.14RS/YS1-112[»]
4P6FX-ray3.60RS/YS1-112[»]
4P70X-ray3.68RS/YS1-112[»]
4TUAX-ray3.60RS/YS1-112[»]
4TUBX-ray3.60RS/YS1-112[»]
4TUCX-ray3.60RS/YS1-112[»]
4TUDX-ray3.60RS/YS1-112[»]
4TUEX-ray3.50RS/YS1-112[»]
4V42X-ray5.50BQ1-112[»]
4V4PX-ray5.50Q1-112[»]
4V4XX-ray5.00BR1-112[»]
4V4YX-ray5.50BR1-112[»]
4V4ZX-ray4.51BR1-112[»]
4V51X-ray2.80BS/DS2-112[»]
4V5AX-ray3.50BS/DS2-112[»]
4V5CX-ray3.30BS/DS1-112[»]
4V5DX-ray3.50BS/DS1-112[»]
4V5EX-ray3.45BS/DS1-112[»]
4V5FX-ray3.60BS/DS1-112[»]
4V5GX-ray3.60BS/DS1-112[»]
4V5JX-ray3.10BS/DS1-112[»]
4V5KX-ray3.20BS/DS1-112[»]
4V5LX-ray3.10BS1-112[»]
4V5Melectron microscopy7.80BS1-112[»]
4V5Nelectron microscopy7.60BS1-112[»]
4V5PX-ray3.10BS/DS1-112[»]
4V5QX-ray3.10BS/DS1-112[»]
4V5RX-ray3.10BS/DS1-112[»]
4V5SX-ray3.10BS/DS1-112[»]
4V68electron microscopy6.40BS11-109[»]
4V6AX-ray3.10BS/DS1-112[»]
4V6FX-ray3.10AQ/DQ1-112[»]
4V6GX-ray3.50BQ/DQ1-112[»]
4V7JX-ray3.30AS/BS1-112[»]
4V7KX-ray3.60AS/BS1-112[»]
4V7LX-ray3.00BS/DS1-112[»]
4V7MX-ray3.45BS/DS1-112[»]
4V7WX-ray3.00BS/DS1-112[»]
4V7XX-ray3.00BS/DS1-112[»]
4V7YX-ray3.00BS/DS1-112[»]
4V7ZX-ray3.10BS/DS1-112[»]
4V87X-ray3.10AQ/DQ2-112[»]
4V8AX-ray3.20AS/BS1-112[»]
4V8BX-ray3.00BQ/DQ1-112[»]
4V8CX-ray3.30AQ/BQ1-112[»]
4V8DX-ray3.00BQ/DQ1-112[»]
4V8EX-ray3.30AQ/CQ1-112[»]
4V8FX-ray3.30AQ/DQ1-112[»]
4V8GX-ray3.00BS/DS1-112[»]
4V8HX-ray3.10BS/DS1-112[»]
4V8IX-ray2.70BS/DS1-112[»]
4V8JX-ray3.90BS/DS1-112[»]
4V8NX-ray3.10BS/DS1-112[»]
4V8OX-ray3.80BS1-112[»]
4V8QX-ray3.10AS1-112[»]
4V8UX-ray3.70BS/DS1-112[»]
4V8XX-ray3.35BS/DS1-112[»]
4V90X-ray2.95BS2-112[»]
4V95X-ray3.20BS/DS1-112[»]
4V97X-ray3.52BS/DS1-112[»]
4V9AX-ray3.30BQ/DQ1-112[»]
4V9BX-ray3.10BQ/DQ1-112[»]
4V9HX-ray2.86BS1-112[»]
4V9IX-ray3.30BS/DS11-108[»]
4V9RX-ray3.00BS/DS1-112[»]
4V9SX-ray3.10BS/DS1-112[»]
4W2EX-ray2.90S1-112[»]
4W2FX-ray2.40BS/DS1-112[»]
4W2GX-ray2.55BS/DS1-112[»]
4W2HX-ray2.70BS/DS1-112[»]
4W2IX-ray2.70BS/DS1-112[»]
4WPOX-ray2.80AS/CS1-112[»]
4WQFX-ray2.80AS/CS1-112[»]
4WQUX-ray2.80AS/CS1-112[»]
4WQYX-ray2.80AS/CS1-112[»]
4WWEX-ray3.40R11-108[»]
4WWTX-ray3.40R11-108[»]
4Y4OX-ray2.301S/2S1-112[»]
4Y4PX-ray2.501S/2S1-112[»]
ProteinModelPortaliQ5SHQ4.
SMRiQ5SHQ4. Positions 3-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71499; BAD71499; BAD71499.
GeneIDi3169978.
KEGGittj:TTHA1676.
PATRICi23958307. VBITheThe93045_1646.

Phylogenomic databases

eggNOGiCOG0256.
HOGENOMiHOG000248742.
KOiK02881.
OMAiSYRYHGR.
OrthoDBiEOG64NB48.
PhylomeDBiQ5SHQ4.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1715-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHQ4.

Family and domain databases

HAMAPiMF_01337_B. Ribosomal_L18_B.
InterProiIPR005484. Ribosomal_L18/L5.
IPR004389. Ribosomal_L18_bac-type.
[Graphical view]
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00060. L18_bact. 1 hit.
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, purification and partial sequence of four Thermus thermophilus 5S rRNA binding proteins."
    Kim J.-S., Boysen R.I., Schroeder W., Erdmann V.A., Gessner R.V.
    Endocyt. Cell Res. 11:177-194(1996)
    Cited for: PROTEIN SEQUENCE OF 2-24, ISOLATION OF 5S RRNA-ASSOCIATED COMPLEXES.
  3. "The isolation and complete amino acid sequence of the ribosomal protein L36 from Thermus thermophilus and its zinc-binding motif."
    Boysen R.I., Lorenz S., Kim J.S., Schroeder W.F.K.J., Erdmann V.A.
    Endocyt. Cell Res. 11:41-58(1995)
    Cited for: PROTEIN SEQUENCE OF 2-19.
  4. "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 2-16.
  5. "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.
  6. "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.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL18_THET8
AccessioniPrimary (citable) accession number: Q5SHQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 90 of the entry and version 3 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.