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Q5SHQ0 (RL5_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L5
Gene names
Name:rplE
Ordered Locus Names:TTHA1680
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (forming bridge B1b) connecting the head of the 30S subunit to the top of the 50S subunit. The bridge itself contacts the P site tRNA and is implicated in movement during ribosome translocation. Also contacts the P site tRNA independently of the intersubunit bridge; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. HAMAP-Rule MF_01333_B

Subunit structure

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 (TL5) subcomplex; has also been isolated as a complex with 5S rRNA, RL25 (TL5) and DNA binding protein II. Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13; this bridge is straddled by the 5S rRNA. Contacts the P site tRNA. Ref.8

Sequence similarities

Belongs to the ribosomal protein L5P family.

Caution

Note that in Ref.3 it was shown that the initiator methionine is not removed, in Ref.5 it was shown the initiator methionine is removed, and the mass determined in Ref.6 is compatible with initiator methionine removal.

In Ref.5 there is uncertainty about the number of Arg residues at position 10 and whether position 25 is Pro or Tyr.

Mass spectrometry

Molecular mass is 20900 Da from positions 2 - 182. Determined by MALDI. Ref.6

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4 Ref.5
Chain2 – 18218150S ribosomal protein L5 HAMAP-Rule MF_01333_B
PRO_0000125014

Secondary structure

......................................... 182
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHQ0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 69A3361F6825929B

FASTA18221,030
        10         20         30         40         50         60 
MPLDVALKRK YYEEVRPELI RRFGYQNVWE VPRLEKVVIN QGLGEAKEDA RILEKAAQEL 

        70         80         90        100        110        120 
ALITGQKPAV TRAKKSISNF KLRKGMPIGL RVTLRRDRMW IFLEKLLNVA LPRIRDFRGL 

       130        140        150        160        170        180 
NPNSFDGRGN YNLGLREQLI FPEITYDMVD ALRGMDIAVV TTAETDEEAR ALLELLGFPF 


RK 

« Hide

References

« Hide 'large scale' references
[1]"Comparative analysis of ribosomal protein L5 sequences from bacteria of the genus Thermus."
Jahn O., Hartmann R.K., Boeckh T., Erdmann V.A.
Biochimie 73:669-678(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"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 2-44, ISOLATION OF 5S RRNA-ASSOCIATED COMPLEXES.
[4]"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 2-41.
[5]"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 2-28.
[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]"Crystal structure of the ribosome at 5.5 A resolution."
Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F.
Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME, INTERSUBUNIT BRIDGE FORMATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD71503.1.
RefSeqYP_144946.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50G1-182[»]
1YL3X-ray5.50G32-38[»]
2HGJX-ray5.00G1-182[»]
2HGQX-ray5.50G1-182[»]
2HGUX-ray4.51G1-182[»]
2J01X-ray2.80G2-182[»]
2J03X-ray2.80G2-182[»]
2V47X-ray3.50G2-182[»]
2V49X-ray3.50G2-182[»]
2WDIX-ray3.30G1-182[»]
2WDJX-ray3.30G1-182[»]
2WDLX-ray3.50G1-182[»]
2WDNX-ray3.50G1-182[»]
2WH2X-ray3.45G1-182[»]
2WH4X-ray3.45G1-182[»]
2WRJX-ray3.60G1-182[»]
2WRLX-ray3.60G1-182[»]
2WROX-ray3.60G1-182[»]
2WRRX-ray3.60G1-182[»]
2X9SX-ray3.10G1-182[»]
2X9UX-ray3.10G1-182[»]
2XG0X-ray3.20G1-182[»]
2XG2X-ray3.20G1-182[»]
2XQEX-ray3.10G1-182[»]
2XTGelectron microscopy7.80G1-182[»]
2XUXelectron microscopy7.60G1-182[»]
2Y0VX-ray3.10G1-182[»]
2Y0XX-ray3.10G1-182[»]
2Y0ZX-ray3.10G1-182[»]
2Y11X-ray3.10G1-182[»]
2Y13X-ray3.10G1-182[»]
2Y15X-ray3.10G1-182[»]
2Y17X-ray3.10G1-182[»]
2Y19X-ray3.10G1-182[»]
3FINelectron microscopy6.40G2-182[»]
3HUXX-ray3.10G1-182[»]
3HUZX-ray3.10G1-182[»]
3I8FX-ray3.10G1-182[»]
3I8IX-ray3.10G1-182[»]
3I9CX-ray3.50G1-182[»]
3I9EX-ray3.50G1-182[»]
3KIRX-ray3.30G1-182[»]
3KITX-ray3.30G1-182[»]
3KIWX-ray3.60G1-182[»]
3KIYX-ray3.60G1-182[»]
3KNIX-ray3.00G1-182[»]
3KNKX-ray3.00G1-182[»]
3KNMX-ray3.45G1-182[»]
3KNOX-ray3.45G1-182[»]
3TVEX-ray3.10G2-182[»]
3TVHX-ray3.10G2-182[»]
3UXQX-ray3.20G1-182[»]
3UXRX-ray3.20G1-182[»]
3UYEX-ray3.00G1-182[»]
3UYGX-ray3.00G1-182[»]
3UZ1X-ray3.30G1-182[»]
3UZ2X-ray3.30G1-182[»]
3UZ8X-ray3.00G1-182[»]
3UZ9X-ray3.00G1-182[»]
3UZFX-ray3.30G1-182[»]
3UZHX-ray3.30G1-182[»]
3UZKX-ray3.30G1-182[»]
3UZNX-ray3.30G1-182[»]
3V23X-ray3.00G1-182[»]
3V25X-ray3.00G1-182[»]
3V27X-ray3.10G1-182[»]
3V29X-ray3.10G1-182[»]
3V2DX-ray2.70G1-182[»]
3V2FX-ray2.70G1-182[»]
3V6WX-ray3.90G1-182[»]
3V6XX-ray3.90G1-182[»]
3ZN9X-ray3.10G1-182[»]
3ZNEX-ray3.10G1-182[»]
3ZVPX-ray3.80G1-182[»]
4ABSX-ray3.10G1-182[»]
4B8GX-ray3.70G1-182[»]
4B8IX-ray3.70G1-182[»]
4BTDX-ray2.95G2-182[»]
4BYCX-ray3.35G1-182[»]
4BYEX-ray3.35G1-182[»]
4DHAX-ray3.20G1-182[»]
4DHCX-ray3.20G1-182[»]
4EJBX-ray3.52G1-182[»]
4EJCX-ray3.52G1-182[»]
4G5LX-ray3.30G1-182[»]
4G5NX-ray3.30G1-182[»]
4G5UX-ray3.10G1-182[»]
4G5WX-ray3.10G1-182[»]
4JUXX-ray2.86G1-182[»]
4K0MX-ray3.30G2-182[»]
4K0QX-ray3.30G2-182[»]
4NVVX-ray3.00G1-182[»]
4NVXX-ray3.00G1-182[»]
4NVZX-ray3.10G1-182[»]
4NW1X-ray3.10G1-182[»]
ProteinModelPortalQ5SHQ0.
SMRQ5SHQ0. Positions 1-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71503; BAD71503; BAD71503.
GeneID3169803.
KEGGttj:TTHA1680.
PATRIC23958315. VBITheThe93045_1650.

Phylogenomic databases

eggNOGCOG0094.
HOGENOMHOG000231311.
KOK02931.
OMATEQLIFP.
OrthoDBEOG6M9F1R.
PhylomeDBQ5SHQ0.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1719-MONOMER.

Family and domain databases

Gene3D3.30.1440.10. 1 hit.
HAMAPMF_01333_B. Ribosomal_L5_B.
InterProIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERPTHR11994. PTHR11994. 1 hit.
PfamPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMSSF55282. SSF55282. 1 hit.
PROSITEPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SHQ0.

Entry information

Entry nameRL5_THET8
AccessionPrimary (citable) accession number: Q5SHQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references