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Protein

50S ribosomal protein L15

Gene

rplO

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the 23S rRNA.By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1712-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L15
Gene namesi
Name:rplO
Ordered Locus Names:TTHA1673
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15015050S ribosomal protein L15PRO_0000104846Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi300852.TTHA1673.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi7 – 93Combined sources
Turni10 – 123Combined sources
Helixi13 – 153Combined sources
Helixi23 – 253Combined sources
Turni29 – 324Combined sources
Helixi37 – 404Combined sources
Beta strandi41 – 433Combined sources
Turni48 – 503Combined sources
Beta strandi53 – 553Combined sources
Turni58 – 614Combined sources
Beta strandi80 – 845Combined sources
Helixi85 – 884Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 953Combined sources
Helixi97 – 1026Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi111 – 1155Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi124 – 1307Combined sources
Helixi132 – 1409Combined sources
Beta strandi144 – 1474Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44P1-150[»]
1VY4X-ray2.60P1-150[»]
1VY5X-ray2.55P1-150[»]
1VY6X-ray2.90P1-150[»]
1VY7X-ray2.80P1-150[»]
4L47X-ray3.22P1-150[»]
4L71X-ray3.90P1-150[»]
4LELX-ray3.90P1-150[»]
4LFZX-ray3.92P1-150[»]
4LNTX-ray2.94P1-150[»]
4LSKX-ray3.48P1-150[»]
4LT8X-ray3.14P1-150[»]
4P6FX-ray3.60K1-150[»]
4P70X-ray3.68P1-150[»]
4V42X-ray5.50O1-150[»]
4V4PX-ray5.50O1-150[»]
4V4XX-ray5.00O1-150[»]
4V4YX-ray5.50O1-150[»]
4V4ZX-ray4.51O1-150[»]
4V51X-ray2.80P1-150[»]
4V5AX-ray3.80P1-150[»]
4V5CX-ray3.30P1-150[»]
4V5DX-ray3.50P1-150[»]
4V5EX-ray3.45P1-150[»]
4V5FX-ray3.60P1-150[»]
4V5GX-ray3.60P1-150[»]
4V5JX-ray3.10P1-150[»]
4V5KX-ray3.20P1-150[»]
4V5LX-ray3.10P1-150[»]
4V5Melectron microscopy7.80P1-150[»]
4V5Nelectron microscopy7.60P1-150[»]
4V5PX-ray3.10P1-150[»]
4V5QX-ray3.10P1-150[»]
4V5RX-ray3.10P1-150[»]
4V5SX-ray3.10P1-150[»]
4V68electron microscopy6.40P5-150[»]
4V6AX-ray3.10P1-150[»]
4V6FX-ray3.10O1-150[»]
4V6GX-ray3.50O1-150[»]
4V7JX-ray3.30P1-150[»]
4V7KX-ray3.60P1-150[»]
4V7LX-ray3.00P1-150[»]
4V7MX-ray3.45P1-150[»]
4V87X-ray3.10O1-150[»]
4V8AX-ray3.20P1-150[»]
4V8BX-ray3.00O1-150[»]
4V8CX-ray3.30O1-150[»]
4V8DX-ray3.00O1-150[»]
4V8EX-ray3.30O1-150[»]
4V8FX-ray3.30O1-150[»]
4V8GX-ray3.00P1-150[»]
4V8HX-ray3.10P1-150[»]
4V8IX-ray2.70P1-150[»]
4V8JX-ray3.90P1-150[»]
4V8NX-ray3.10P1-150[»]
4V8OX-ray3.80P1-150[»]
4V8QX-ray3.10P1-150[»]
4V8UX-ray3.70P1-150[»]
4V8XX-ray3.35P1-150[»]
4V90X-ray2.95P2-150[»]
4V95X-ray3.20P1-150[»]
4V97X-ray3.52P1-150[»]
4V9AX-ray3.30O1-150[»]
4V9BX-ray3.10O1-150[»]
4V9HX-ray2.86P1-150[»]
4V9IX-ray3.30P5-150[»]
4V9RX-ray3.00P1-150[»]
4V9SX-ray3.10P1-150[»]
4W2EX-ray2.90P1-150[»]
4W2FX-ray2.40P1-150[»]
4W2GX-ray2.55P1-150[»]
4W2HX-ray2.70P1-150[»]
4W2IX-ray2.70P1-150[»]
ProteinModelPortaliQ5SHQ7.
SMRiQ5SHQ7. Positions 5-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHQ7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiCOG0200.
HOGENOMiHOG000231262.
KOiK02876.
OMAiTNPFRTE.
OrthoDBiEOG6CGCM5.
PhylomeDBiQ5SHQ7.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SHQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSDLRPNP GANKRRKRVG RGPGSGHGKT ATRGHKGQKS RSGGLKDPRR
60 70 80 90 100
FEGGRSTTLM RLPKRGMQGQ VPGEIKRPRY QGVNLKDLAR FEGEVTPELL
110 120 130 140 150
VRAGLLKKGY RLKILGEGEA KPLKVVAHAF SKSALEKLKA AGGEPVLLEA
Length:150
Mass (Da):16,281
Last modified:December 21, 2004 - v1
Checksum:i0175AF33F530AD4F
GO

Mass spectrometryi

Molecular mass is 16284 Da from positions 1 - 150. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71496.1.
RefSeqiWP_011173703.1. NC_006461.1.
YP_144939.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71496; BAD71496; BAD71496.
GeneIDi3168730.
KEGGittj:TTHA1673.
PATRICi23958301. VBITheThe93045_1643.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71496.1.
RefSeqiWP_011173703.1. NC_006461.1.
YP_144939.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44P1-150[»]
1VY4X-ray2.60P1-150[»]
1VY5X-ray2.55P1-150[»]
1VY6X-ray2.90P1-150[»]
1VY7X-ray2.80P1-150[»]
4L47X-ray3.22P1-150[»]
4L71X-ray3.90P1-150[»]
4LELX-ray3.90P1-150[»]
4LFZX-ray3.92P1-150[»]
4LNTX-ray2.94P1-150[»]
4LSKX-ray3.48P1-150[»]
4LT8X-ray3.14P1-150[»]
4P6FX-ray3.60K1-150[»]
4P70X-ray3.68P1-150[»]
4V42X-ray5.50O1-150[»]
4V4PX-ray5.50O1-150[»]
4V4XX-ray5.00O1-150[»]
4V4YX-ray5.50O1-150[»]
4V4ZX-ray4.51O1-150[»]
4V51X-ray2.80P1-150[»]
4V5AX-ray3.80P1-150[»]
4V5CX-ray3.30P1-150[»]
4V5DX-ray3.50P1-150[»]
4V5EX-ray3.45P1-150[»]
4V5FX-ray3.60P1-150[»]
4V5GX-ray3.60P1-150[»]
4V5JX-ray3.10P1-150[»]
4V5KX-ray3.20P1-150[»]
4V5LX-ray3.10P1-150[»]
4V5Melectron microscopy7.80P1-150[»]
4V5Nelectron microscopy7.60P1-150[»]
4V5PX-ray3.10P1-150[»]
4V5QX-ray3.10P1-150[»]
4V5RX-ray3.10P1-150[»]
4V5SX-ray3.10P1-150[»]
4V68electron microscopy6.40P5-150[»]
4V6AX-ray3.10P1-150[»]
4V6FX-ray3.10O1-150[»]
4V6GX-ray3.50O1-150[»]
4V7JX-ray3.30P1-150[»]
4V7KX-ray3.60P1-150[»]
4V7LX-ray3.00P1-150[»]
4V7MX-ray3.45P1-150[»]
4V87X-ray3.10O1-150[»]
4V8AX-ray3.20P1-150[»]
4V8BX-ray3.00O1-150[»]
4V8CX-ray3.30O1-150[»]
4V8DX-ray3.00O1-150[»]
4V8EX-ray3.30O1-150[»]
4V8FX-ray3.30O1-150[»]
4V8GX-ray3.00P1-150[»]
4V8HX-ray3.10P1-150[»]
4V8IX-ray2.70P1-150[»]
4V8JX-ray3.90P1-150[»]
4V8NX-ray3.10P1-150[»]
4V8OX-ray3.80P1-150[»]
4V8QX-ray3.10P1-150[»]
4V8UX-ray3.70P1-150[»]
4V8XX-ray3.35P1-150[»]
4V90X-ray2.95P2-150[»]
4V95X-ray3.20P1-150[»]
4V97X-ray3.52P1-150[»]
4V9AX-ray3.30O1-150[»]
4V9BX-ray3.10O1-150[»]
4V9HX-ray2.86P1-150[»]
4V9IX-ray3.30P5-150[»]
4V9RX-ray3.00P1-150[»]
4V9SX-ray3.10P1-150[»]
4W2EX-ray2.90P1-150[»]
4W2FX-ray2.40P1-150[»]
4W2GX-ray2.55P1-150[»]
4W2HX-ray2.70P1-150[»]
4W2IX-ray2.70P1-150[»]
ProteinModelPortaliQ5SHQ7.
SMRiQ5SHQ7. Positions 5-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71496; BAD71496; BAD71496.
GeneIDi3168730.
KEGGittj:TTHA1673.
PATRICi23958301. VBITheThe93045_1643.

Phylogenomic databases

eggNOGiCOG0200.
HOGENOMiHOG000231262.
KOiK02876.
OMAiTNPFRTE.
OrthoDBiEOG6CGCM5.
PhylomeDBiQ5SHQ7.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1712-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHQ7.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]
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 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 1-15.
  3. "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.
  4. "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.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL15_THET8
AccessioniPrimary (citable) accession number: Q5SHQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 88 of the entry and version 1 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.