Skip Header

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

50S ribosomal protein L5

Gene

rplE

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 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

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
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001250142 – 18250S ribosomal protein L5Add BLAST181

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.

Protein-protein interaction databases

STRINGi300852.TTHA1680.

Structurei

Secondary structure

1182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 12Combined sources7
Helixi15 – 23Combined sources9
Turni28 – 30Combined sources3
Beta strandi34 – 40Combined sources7
Turni48 – 50Combined sources3
Helixi55 – 64Combined sources10
Beta strandi84 – 86Combined sources3
Beta strandi90 – 94Combined sources5
Helixi98 – 113Combined sources16
Beta strandi114 – 116Combined sources3
Beta strandi124 – 136Combined sources13
Beta strandi138 – 144Combined sources7
Turni146 – 148Combined sources3
Beta strandi155 – 162Combined sources8
Helixi166 – 175Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RG/YG1-182[»]
1VY4X-ray2.60BG/DG1-182[»]
1VY5X-ray2.55BG/DG1-182[»]
1VY6X-ray2.90BG/DG1-182[»]
1VY7X-ray2.80BG/DG1-182[»]
4L47X-ray3.22RG/YG1-182[»]
4L71X-ray3.90RG/YG1-182[»]
4LELX-ray3.90RG/YG1-182[»]
4LFZX-ray3.92RG/YG1-182[»]
4LNTX-ray2.94RG/YG1-182[»]
4LSKX-ray3.48RG/YG1-182[»]
4LT8X-ray3.14RG/YG1-182[»]
4P6FX-ray3.60RG/YG1-182[»]
4P70X-ray3.68RG/YG1-182[»]
4TUAX-ray3.60RG/YG1-182[»]
4TUBX-ray3.60RG/YG1-182[»]
4TUCX-ray3.60RG/YG1-182[»]
4TUDX-ray3.60RG/YG1-182[»]
4TUEX-ray3.50RG/YG1-182[»]
4V42X-ray5.50RG1-182[»]
4V4PX-ray5.50G32-38[»]
4V4XX-ray5.00G1-182[»]
4V4YX-ray5.50G1-182[»]
4V4ZX-ray4.51G1-182[»]
4V51X-ray2.80BG/DG2-182[»]
4V5AX-ray3.50BG/DG2-182[»]
4V5CX-ray3.30BG/DG1-182[»]
4V5DX-ray3.50BG/DG1-182[»]
4V5EX-ray3.45BG/DG1-182[»]
4V5FX-ray3.60BG/DG1-182[»]
4V5GX-ray3.60BG/DG1-182[»]
4V5JX-ray3.10BG/DG1-182[»]
4V5KX-ray3.20BG/DG1-182[»]
4V5LX-ray3.10BG1-182[»]
4V5Melectron microscopy7.80BG1-182[»]
4V5Nelectron microscopy7.60BG1-182[»]
4V5PX-ray3.10BG/DG1-182[»]
4V5QX-ray3.10BG/DG1-182[»]
4V5RX-ray3.10BG/DG1-182[»]
4V5SX-ray3.10BG/DG1-182[»]
4V68electron microscopy6.40BG2-182[»]
4V6AX-ray3.10BG/DG1-182[»]
4V6FX-ray3.10AG/DG1-182[»]
4V6GX-ray3.50BG/DG1-182[»]
4V7JX-ray3.30AG/BG1-182[»]
4V7KX-ray3.60AG/BG1-182[»]
4V7LX-ray3.00BG/DG1-182[»]
4V7MX-ray3.45BG/DG1-182[»]
4V7WX-ray3.00BG/DG1-182[»]
4V7XX-ray3.00BG/DG1-182[»]
4V7YX-ray3.00BG/DG1-182[»]
4V7ZX-ray3.10BG/DG1-182[»]
4V87X-ray3.10AG/DG2-182[»]
4V8AX-ray3.20AG/BG1-182[»]
4V8BX-ray3.00BG/DG1-182[»]
4V8CX-ray3.30AG/BG1-182[»]
4V8DX-ray3.00BG/DG1-182[»]
4V8EX-ray3.30AG/CG1-182[»]
4V8FX-ray3.30AG/DG1-182[»]
4V8GX-ray3.00BG/DG1-182[»]
4V8HX-ray3.10BG/DG1-182[»]
4V8IX-ray2.70BG/DG1-182[»]
4V8JX-ray3.90BG/DG1-182[»]
4V8NX-ray3.10BG/DG1-182[»]
4V8OX-ray3.80BG1-182[»]
4V8QX-ray3.10AG1-182[»]
4V8UX-ray3.70BG/DG1-182[»]
4V8XX-ray3.35BG/DG1-182[»]
4V90X-ray2.95BG2-182[»]
4V95X-ray3.20BG/DG1-182[»]
4V97X-ray3.52BG/DG1-182[»]
4V9AX-ray3.30BG/DG1-182[»]
4V9BX-ray3.10BG/DG1-182[»]
4V9HX-ray2.86BG1-182[»]
4V9IX-ray3.30BG/DG2-182[»]
4V9RX-ray3.00BG/DG1-182[»]
4V9SX-ray3.10BG/DG1-182[»]
4W2EX-ray2.90G1-182[»]
4W2FX-ray2.40BG/DG1-182[»]
4W2GX-ray2.55BG/DG1-182[»]
4W2HX-ray2.70BG/DG1-182[»]
4W2IX-ray2.70BG/DG1-182[»]
4W4GX-ray3.30RG/YG1-182[»]
4WPOX-ray2.80AG/CG1-182[»]
4WQ1X-ray3.1041/492-182[»]
4WQFX-ray2.80AG/CG1-182[»]
4WQRX-ray3.1541/491-182[»]
4WQUX-ray2.80AG/CG1-182[»]
4WQYX-ray2.80AG/CG1-182[»]
4WR6X-ray3.0541/491-182[»]
4WRAX-ray3.0541/491-182[»]
4WROX-ray3.05411-182[»]
4WSDX-ray2.9541/491-182[»]
4WSMX-ray3.3041/491-182[»]
4WT1X-ray3.0541/491-182[»]
4WT8X-ray3.40CE/DE2-182[»]
4WU1X-ray3.2041/491-182[»]
4WZDX-ray3.1041/491-182[»]
4WZOX-ray3.3041/491-182[»]
4Y4OX-ray2.301G/2G1-182[»]
4Y4PX-ray2.501G/2G1-182[»]
4YPBX-ray3.40RG/YG1-182[»]
4YZVX-ray3.10RG/YG1-182[»]
4Z3SX-ray2.651G/2G1-182[»]
4Z8CX-ray2.901G/2G1-182[»]
4ZERX-ray3.101G/2G2-182[»]
4ZSNX-ray3.60RG/YG1-182[»]
5A9Zelectron microscopy4.70AG1-182[»]
5AA0electron microscopy5.00AG1-182[»]
5CZPX-ray3.30RG/YG1-182[»]
5D8BX-ray3.63D/ZA6-182[»]
5DFEX-ray3.10RG/YG1-182[»]
5DOXX-ray3.101G/2G1-182[»]
5DOYX-ray2.601G/2G1-182[»]
5E7KX-ray3.2041/491-182[»]
5E81X-ray2.9541/491-182[»]
5EL4X-ray3.1541/491-182[»]
5EL5X-ray3.1541/491-182[»]
5EL6X-ray3.1041/491-182[»]
5EL7X-ray3.1541/491-182[»]
5F8KX-ray2.801G/2G2-182[»]
5FDUX-ray2.901G/2G2-182[»]
5FDVX-ray2.801G/2G2-182[»]
5HAUX-ray3.001G/2G1-182[»]
5HCPX-ray2.891G/2G1-182[»]
5HCQX-ray2.801G/2G1-182[»]
5HCRX-ray2.801G/2G1-182[»]
5HD1X-ray2.701G/2G1-182[»]
5IB7X-ray2.9941/491-182[»]
5IB8X-ray3.1341/491-182[»]
5IBBX-ray2.9641/491-182[»]
5IMQelectron microscopy3.80d1-182[»]
5IMRelectron microscopy-d1-182[»]
5J30X-ray3.20RG/YG1-182[»]
5J3CX-ray3.04RG/YG1-182[»]
5J4BX-ray2.601G/2G1-182[»]
5J4CX-ray2.801G/2G1-182[»]
5J8BX-ray2.60G1-182[»]
ProteinModelPortaliQ5SHQ0.
SMRiQ5SHQ0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHQ0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiENOG4105CW6. Bacteria.
COG0094. LUCA.
HOGENOMiHOG000231311.
KOiK02931.
OMAiEQVMFHE.
PhylomeDBiQ5SHQ0.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
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

        10         20         30         40         50
MPLDVALKRK YYEEVRPELI RRFGYQNVWE VPRLEKVVIN QGLGEAKEDA
60 70 80 90 100
RILEKAAQEL ALITGQKPAV TRAKKSISNF KLRKGMPIGL RVTLRRDRMW
110 120 130 140 150
IFLEKLLNVA LPRIRDFRGL NPNSFDGRGN YNLGLREQLI FPEITYDMVD
160 170 180
ALRGMDIAVV TTAETDEEAR ALLELLGFPF RK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71503.1.
RefSeqiWP_011228843.1. NC_006461.1.
YP_144946.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RG/YG1-182[»]
1VY4X-ray2.60BG/DG1-182[»]
1VY5X-ray2.55BG/DG1-182[»]
1VY6X-ray2.90BG/DG1-182[»]
1VY7X-ray2.80BG/DG1-182[»]
4L47X-ray3.22RG/YG1-182[»]
4L71X-ray3.90RG/YG1-182[»]
4LELX-ray3.90RG/YG1-182[»]
4LFZX-ray3.92RG/YG1-182[»]
4LNTX-ray2.94RG/YG1-182[»]
4LSKX-ray3.48RG/YG1-182[»]
4LT8X-ray3.14RG/YG1-182[»]
4P6FX-ray3.60RG/YG1-182[»]
4P70X-ray3.68RG/YG1-182[»]
4TUAX-ray3.60RG/YG1-182[»]
4TUBX-ray3.60RG/YG1-182[»]
4TUCX-ray3.60RG/YG1-182[»]
4TUDX-ray3.60RG/YG1-182[»]
4TUEX-ray3.50RG/YG1-182[»]
4V42X-ray5.50RG1-182[»]
4V4PX-ray5.50G32-38[»]
4V4XX-ray5.00G1-182[»]
4V4YX-ray5.50G1-182[»]
4V4ZX-ray4.51G1-182[»]
4V51X-ray2.80BG/DG2-182[»]
4V5AX-ray3.50BG/DG2-182[»]
4V5CX-ray3.30BG/DG1-182[»]
4V5DX-ray3.50BG/DG1-182[»]
4V5EX-ray3.45BG/DG1-182[»]
4V5FX-ray3.60BG/DG1-182[»]
4V5GX-ray3.60BG/DG1-182[»]
4V5JX-ray3.10BG/DG1-182[»]
4V5KX-ray3.20BG/DG1-182[»]
4V5LX-ray3.10BG1-182[»]
4V5Melectron microscopy7.80BG1-182[»]
4V5Nelectron microscopy7.60BG1-182[»]
4V5PX-ray3.10BG/DG1-182[»]
4V5QX-ray3.10BG/DG1-182[»]
4V5RX-ray3.10BG/DG1-182[»]
4V5SX-ray3.10BG/DG1-182[»]
4V68electron microscopy6.40BG2-182[»]
4V6AX-ray3.10BG/DG1-182[»]
4V6FX-ray3.10AG/DG1-182[»]
4V6GX-ray3.50BG/DG1-182[»]
4V7JX-ray3.30AG/BG1-182[»]
4V7KX-ray3.60AG/BG1-182[»]
4V7LX-ray3.00BG/DG1-182[»]
4V7MX-ray3.45BG/DG1-182[»]
4V7WX-ray3.00BG/DG1-182[»]
4V7XX-ray3.00BG/DG1-182[»]
4V7YX-ray3.00BG/DG1-182[»]
4V7ZX-ray3.10BG/DG1-182[»]
4V87X-ray3.10AG/DG2-182[»]
4V8AX-ray3.20AG/BG1-182[»]
4V8BX-ray3.00BG/DG1-182[»]
4V8CX-ray3.30AG/BG1-182[»]
4V8DX-ray3.00BG/DG1-182[»]
4V8EX-ray3.30AG/CG1-182[»]
4V8FX-ray3.30AG/DG1-182[»]
4V8GX-ray3.00BG/DG1-182[»]
4V8HX-ray3.10BG/DG1-182[»]
4V8IX-ray2.70BG/DG1-182[»]
4V8JX-ray3.90BG/DG1-182[»]
4V8NX-ray3.10BG/DG1-182[»]
4V8OX-ray3.80BG1-182[»]
4V8QX-ray3.10AG1-182[»]
4V8UX-ray3.70BG/DG1-182[»]
4V8XX-ray3.35BG/DG1-182[»]
4V90X-ray2.95BG2-182[»]
4V95X-ray3.20BG/DG1-182[»]
4V97X-ray3.52BG/DG1-182[»]
4V9AX-ray3.30BG/DG1-182[»]
4V9BX-ray3.10BG/DG1-182[»]
4V9HX-ray2.86BG1-182[»]
4V9IX-ray3.30BG/DG2-182[»]
4V9RX-ray3.00BG/DG1-182[»]
4V9SX-ray3.10BG/DG1-182[»]
4W2EX-ray2.90G1-182[»]
4W2FX-ray2.40BG/DG1-182[»]
4W2GX-ray2.55BG/DG1-182[»]
4W2HX-ray2.70BG/DG1-182[»]
4W2IX-ray2.70BG/DG1-182[»]
4W4GX-ray3.30RG/YG1-182[»]
4WPOX-ray2.80AG/CG1-182[»]
4WQ1X-ray3.1041/492-182[»]
4WQFX-ray2.80AG/CG1-182[»]
4WQRX-ray3.1541/491-182[»]
4WQUX-ray2.80AG/CG1-182[»]
4WQYX-ray2.80AG/CG1-182[»]
4WR6X-ray3.0541/491-182[»]
4WRAX-ray3.0541/491-182[»]
4WROX-ray3.05411-182[»]
4WSDX-ray2.9541/491-182[»]
4WSMX-ray3.3041/491-182[»]
4WT1X-ray3.0541/491-182[»]
4WT8X-ray3.40CE/DE2-182[»]
4WU1X-ray3.2041/491-182[»]
4WZDX-ray3.1041/491-182[»]
4WZOX-ray3.3041/491-182[»]
4Y4OX-ray2.301G/2G1-182[»]
4Y4PX-ray2.501G/2G1-182[»]
4YPBX-ray3.40RG/YG1-182[»]
4YZVX-ray3.10RG/YG1-182[»]
4Z3SX-ray2.651G/2G1-182[»]
4Z8CX-ray2.901G/2G1-182[»]
4ZERX-ray3.101G/2G2-182[»]
4ZSNX-ray3.60RG/YG1-182[»]
5A9Zelectron microscopy4.70AG1-182[»]
5AA0electron microscopy5.00AG1-182[»]
5CZPX-ray3.30RG/YG1-182[»]
5D8BX-ray3.63D/ZA6-182[»]
5DFEX-ray3.10RG/YG1-182[»]
5DOXX-ray3.101G/2G1-182[»]
5DOYX-ray2.601G/2G1-182[»]
5E7KX-ray3.2041/491-182[»]
5E81X-ray2.9541/491-182[»]
5EL4X-ray3.1541/491-182[»]
5EL5X-ray3.1541/491-182[»]
5EL6X-ray3.1041/491-182[»]
5EL7X-ray3.1541/491-182[»]
5F8KX-ray2.801G/2G2-182[»]
5FDUX-ray2.901G/2G2-182[»]
5FDVX-ray2.801G/2G2-182[»]
5HAUX-ray3.001G/2G1-182[»]
5HCPX-ray2.891G/2G1-182[»]
5HCQX-ray2.801G/2G1-182[»]
5HCRX-ray2.801G/2G1-182[»]
5HD1X-ray2.701G/2G1-182[»]
5IB7X-ray2.9941/491-182[»]
5IB8X-ray3.1341/491-182[»]
5IBBX-ray2.9641/491-182[»]
5IMQelectron microscopy3.80d1-182[»]
5IMRelectron microscopy-d1-182[»]
5J30X-ray3.20RG/YG1-182[»]
5J3CX-ray3.04RG/YG1-182[»]
5J4BX-ray2.601G/2G1-182[»]
5J4CX-ray2.801G/2G1-182[»]
5J8BX-ray2.60G1-182[»]
ProteinModelPortaliQ5SHQ0.
SMRiQ5SHQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1680.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CW6. Bacteria.
COG0094. LUCA.
HOGENOMiHOG000231311.
KOiK02931.
OMAiEQVMFHE.
PhylomeDBiQ5SHQ0.

Miscellaneous databases

EvolutionaryTraceiQ5SHQ0.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 115 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 Ref. 3 it was shown that the initiator methionine is not removed, in PubMed:11154066 it was shown the initiator methionine is removed, and the mass determined in PubMed:16287167 is compatible with initiator methionine removal.Curated
In PubMed:11154066 there is uncertainty about the number of Arg residues at position 10 and whether position 25 is Pro or Tyr.Curated

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

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 one 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.