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Q5SHQ0

- RL5_THET8

UniProt

Q5SHQ0 - RL5_THET8

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Protein

50S ribosomal protein L5

Gene
rplE, TTHA1680
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1719-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L5
Gene namesi
Name:rplE
Ordered Locus Names:TTHA1680
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
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 18218150S ribosomal protein L5UniRule annotationPRO_0000125014Add
BLAST

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA1680.

Structurei

Secondary structure

1
182
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127
Helixi15 – 239
Turni28 – 303
Beta strandi34 – 418
Helixi44 – 463
Beta strandi47 – 504
Helixi55 – 6410
Beta strandi69 – 757
Beta strandi78 – 814
Beta strandi84 – 9411
Helixi96 – 10813
Helixi110 – 1134
Beta strandi114 – 1163
Beta strandi118 – 1203
Helixi122 – 1243
Beta strandi127 – 13610
Helixi138 – 1403
Beta strandi141 – 1433
Beta strandi146 – 1483
Beta strandi155 – 1628
Helixi166 – 1749
Turni175 – 1773

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ5SHQ0.
SMRiQ5SHQ0. Positions 1-182.

Miscellaneous databases

EvolutionaryTraceiQ5SHQ0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0094.
HOGENOMiHOG000231311.
KOiK02931.
OMAiTEQLIFP.
OrthoDBiEOG6M9F1R.
PhylomeDBiQ5SHQ0.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5SHQ0-1 [UniParc]FASTAAdd to Basket

« Hide

MPLDVALKRK YYEEVRPELI RRFGYQNVWE VPRLEKVVIN QGLGEAKEDA    50
RILEKAAQEL ALITGQKPAV TRAKKSISNF KLRKGMPIGL RVTLRRDRMW 100
IFLEKLLNVA LPRIRDFRGL NPNSFDGRGN YNLGLREQLI FPEITYDMVD 150
ALRGMDIAVV TTAETDEEAR ALLELLGFPF RK 182
Length:182
Mass (Da):21,030
Last modified:January 23, 2007 - v3
Checksum:i69A3361F6825929B
GO

Mass spectrometryi

Molecular mass is 20900 Da from positions 2 - 182. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD71503.1.
RefSeqiWP_011228843.1. NC_006461.1.
YP_144946.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71503; BAD71503; BAD71503.
GeneIDi3169803.
KEGGittj:TTHA1680.
PATRICi23958315. VBITheThe93045_1650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD71503.1 .
RefSeqi WP_011228843.1. NC_006461.1.
YP_144946.1. 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 G 1-182 [» ]
1YL3 X-ray 5.50 G 32-38 [» ]
2HGJ X-ray 5.00 G 1-182 [» ]
2HGQ X-ray 5.50 G 1-182 [» ]
2HGU X-ray 4.51 G 1-182 [» ]
2J01 X-ray 2.80 G 2-182 [» ]
2J03 X-ray 2.80 G 2-182 [» ]
2V47 X-ray 3.50 G 2-182 [» ]
2V49 X-ray 3.50 G 2-182 [» ]
2WDI X-ray 3.30 G 1-182 [» ]
2WDJ X-ray 3.30 G 1-182 [» ]
2WDL X-ray 3.50 G 1-182 [» ]
2WDN X-ray 3.50 G 1-182 [» ]
2WH2 X-ray 3.45 G 1-182 [» ]
2WH4 X-ray 3.45 G 1-182 [» ]
2WRJ X-ray 3.60 G 1-182 [» ]
2WRL X-ray 3.60 G 1-182 [» ]
2WRO X-ray 3.60 G 1-182 [» ]
2WRR X-ray 3.60 G 1-182 [» ]
2X9S X-ray 3.10 G 1-182 [» ]
2X9U X-ray 3.10 G 1-182 [» ]
2XG0 X-ray 3.20 G 1-182 [» ]
2XG2 X-ray 3.20 G 1-182 [» ]
2XQE X-ray 3.10 G 1-182 [» ]
2XTG electron microscopy 7.80 G 1-182 [» ]
2XUX electron microscopy 7.60 G 1-182 [» ]
2Y0V X-ray 3.10 G 1-182 [» ]
2Y0X X-ray 3.10 G 1-182 [» ]
2Y0Z X-ray 3.10 G 1-182 [» ]
2Y11 X-ray 3.10 G 1-182 [» ]
2Y13 X-ray 3.10 G 1-182 [» ]
2Y15 X-ray 3.10 G 1-182 [» ]
2Y17 X-ray 3.10 G 1-182 [» ]
2Y19 X-ray 3.10 G 1-182 [» ]
3FIN electron microscopy 6.40 G 2-182 [» ]
3HUX X-ray 3.10 G 1-182 [» ]
3HUZ X-ray 3.10 G 1-182 [» ]
3I8F X-ray 3.10 G 1-182 [» ]
3I8I X-ray 3.10 G 1-182 [» ]
3I9C X-ray 3.50 G 1-182 [» ]
3I9E X-ray 3.50 G 1-182 [» ]
3KIR X-ray 3.30 G 1-182 [» ]
3KIT X-ray 3.30 G 1-182 [» ]
3KIW X-ray 3.60 G 1-182 [» ]
3KIY X-ray 3.60 G 1-182 [» ]
3KNI X-ray 3.00 G 1-182 [» ]
3KNK X-ray 3.00 G 1-182 [» ]
3KNM X-ray 3.45 G 1-182 [» ]
3KNO X-ray 3.45 G 1-182 [» ]
3TVE X-ray 3.10 G 2-182 [» ]
3TVH X-ray 3.10 G 2-182 [» ]
3UXQ X-ray 3.20 G 1-182 [» ]
3UXR X-ray 3.20 G 1-182 [» ]
3UYE X-ray 3.00 G 1-182 [» ]
3UYG X-ray 3.00 G 1-182 [» ]
3UZ1 X-ray 3.30 G 1-182 [» ]
3UZ2 X-ray 3.30 G 1-182 [» ]
3UZ8 X-ray 3.00 G 1-182 [» ]
3UZ9 X-ray 3.00 G 1-182 [» ]
3UZF X-ray 3.30 G 1-182 [» ]
3UZH X-ray 3.30 G 1-182 [» ]
3UZK X-ray 3.30 G 1-182 [» ]
3UZN X-ray 3.30 G 1-182 [» ]
3V23 X-ray 3.00 G 1-182 [» ]
3V25 X-ray 3.00 G 1-182 [» ]
3V27 X-ray 3.10 G 1-182 [» ]
3V29 X-ray 3.10 G 1-182 [» ]
3V2D X-ray 2.70 G 1-182 [» ]
3V2F X-ray 2.70 G 1-182 [» ]
3V6W X-ray 3.90 G 1-182 [» ]
3V6X X-ray 3.90 G 1-182 [» ]
3ZN9 X-ray 3.10 G 1-182 [» ]
3ZNE X-ray 3.10 G 1-182 [» ]
3ZVP X-ray 3.80 G 1-182 [» ]
4ABS X-ray 3.10 G 1-182 [» ]
4B8G X-ray 3.70 G 1-182 [» ]
4B8I X-ray 3.70 G 1-182 [» ]
4BTD X-ray 2.95 G 2-182 [» ]
4BYC X-ray 3.35 G 1-182 [» ]
4BYE X-ray 3.35 G 1-182 [» ]
4DHA X-ray 3.20 G 1-182 [» ]
4DHC X-ray 3.20 G 1-182 [» ]
4EJB X-ray 3.52 G 1-182 [» ]
4EJC X-ray 3.52 G 1-182 [» ]
4G5L X-ray 3.30 G 1-182 [» ]
4G5N X-ray 3.30 G 1-182 [» ]
4G5U X-ray 3.10 G 1-182 [» ]
4G5W X-ray 3.10 G 1-182 [» ]
4JUX X-ray 2.86 G 1-182 [» ]
4K0M X-ray 3.30 G 2-182 [» ]
4K0Q X-ray 3.30 G 2-182 [» ]
4NVV X-ray 3.00 G 1-182 [» ]
4NVX X-ray 3.00 G 1-182 [» ]
4NVZ X-ray 3.10 G 1-182 [» ]
4NW1 X-ray 3.10 G 1-182 [» ]
ProteinModelPortali Q5SHQ0.
SMRi Q5SHQ0. Positions 1-182.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1680.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71503 ; BAD71503 ; BAD71503 .
GeneIDi 3169803.
KEGGi ttj:TTHA1680.
PATRICi 23958315. VBITheThe93045_1650.

Phylogenomic databases

eggNOGi COG0094.
HOGENOMi HOG000231311.
KOi K02931.
OMAi TEQLIFP.
OrthoDBi EOG6M9F1R.
PhylomeDBi Q5SHQ0.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1719-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SHQ0.

Family and domain databases

Gene3Di 3.30.1440.10. 1 hit.
HAMAPi MF_01333_B. Ribosomal_L5_B.
InterProi IPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view ]
PANTHERi PTHR11994. PTHR11994. 1 hit.
Pfami PF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMi SSF55282. SSF55282. 1 hit.
PROSITEi PS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME, INTERSUBUNIT BRIDGE FORMATION.

Entry informationi

Entry nameiRL5_THET8
AccessioniPrimary (citable) accession number: Q5SHQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Note that in 1 Publication it was shown that the initiator methionine is not removed, in 1 Publication it was shown the initiator methionine is removed, and the mass determined in 1 Publication is compatible with initiator methionine removal.
In 1 Publication there is uncertainty about the number of Arg residues at position 10 and whether position 25 is Pro or Tyr.

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

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