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Q72I16 (RL5_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:TT_C1316
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [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 (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs By similarity. HAMAP-Rule MF_01333

Subunit structure

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome By similarity.

Sequence similarities

Belongs to the ribosomal protein L5P family.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
tRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 18218150S ribosomal protein L5 HAMAP-Rule MF_01333
PRO_0000125013

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q72I16 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C3A8E0CFD884EEEA

FASTA18221,044
        10         20         30         40         50         60 
MPLDLALKRK 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017221 Genomic DNA. Translation: AAS81658.1.
RefSeqYP_005285.1. NC_005835.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VSAX-ray3.71E1-182[»]
1VSPX-ray3.83E1-182[»]
3D5BX-ray3.21G1-182[»]
3D5DX-ray3.21G1-182[»]
3F1FX-ray3.00G1-182[»]
3F1HX-ray3.00G1-182[»]
3MRZX-ray3.62F2-182[»]
3MS1X-ray3.62F2-182[»]
3PYOX-ray3.50F2-182[»]
3PYRX-ray3.50F2-182[»]
3PYTX-ray3.40F2-182[»]
3PYVX-ray3.40F2-182[»]
4KBUX-ray3.86G2-182[»]
4KBWX-ray3.86G2-182[»]
4KCZX-ray3.50G2-182[»]
4KD2X-ray3.50G2-182[»]
4KD9X-ray3.50G2-182[»]
4KDBX-ray3.50G2-182[»]
4KDHX-ray4.00G2-182[»]
4KDKX-ray4.00G2-182[»]
4KFIX-ray3.40G2-182[»]
4KFLX-ray3.40G2-182[»]
4L6JX-ray3.40G2-182[»]
4L6LX-ray3.40G2-182[»]
ProteinModelPortalQ72I16.
SMRQ72I16. Positions 3-182.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS81658; AAS81658; TT_C1316.
GeneID2775564.
KEGGtth:TTC1316.
PATRIC23953039. VBITheThe54392_1308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0094.
KOK02931.
OMAGMPIGAH.
OrthoDBEOG6M9F1R.
ProtClustDBPRK00010.

Enzyme and pathway databases

BioCycTTHE262724:GCAT-1331-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

EvolutionaryTraceQ72I16.

Entry information

Entry nameRL5_THET2
AccessionPrimary (citable) accession number: Q72I16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 69 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