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Protein

50S ribosomal protein L15

Gene

rplO

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the 23S rRNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2158-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L15
Gene namesi
Name:rplO
Ordered Locus Names:DR_2115
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15615650S ribosomal protein L15PRO_0000104716Add
BLAST

Proteomic databases

PRIDEiQ9RSK9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts proteins L4, L21 and L35.6 Publications

Protein-protein interaction databases

STRINGi243230.DR_2115.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 143Combined sources
Beta strandi19 – 213Combined sources
Beta strandi23 – 264Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 363Combined sources
Turni37 – 393Combined sources
Beta strandi44 – 463Combined sources
Beta strandi51 – 533Combined sources
Helixi56 – 594Combined sources
Beta strandi73 – 764Combined sources
Helixi77 – 804Combined sources
Turni82 – 843Combined sources
Helixi92 – 976Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1253Combined sources
Helixi127 – 1348Combined sources
Turni135 – 1373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-J68-145[»]
1NKWX-ray3.10J1-156[»]
1NWXX-ray3.50J1-156[»]
1NWYX-ray3.30J1-156[»]
1SM1X-ray3.42J1-156[»]
1XBPX-ray3.50J1-156[»]
2ZJPX-ray3.70I1-156[»]
2ZJQX-ray3.30I1-156[»]
2ZJRX-ray2.91I1-156[»]
3CF5X-ray3.30I1-156[»]
3DLLX-ray3.50I1-156[»]
3PIOX-ray3.25I1-156[»]
3PIPX-ray3.45I1-156[»]
4IO9X-ray3.20I1-156[»]
4IOAX-ray3.20I1-156[»]
4IOCX-ray3.60I1-156[»]
4U67X-ray3.65I1-156[»]
4V49X-ray8.70J4-144[»]
4V4AX-ray9.50J4-144[»]
4V4GX-ray11.50M4-144[»]
4WFNX-ray3.54I1-156[»]
5DM6X-ray2.90I4-144[»]
5DM7X-ray3.00I4-144[»]
ProteinModelPortaliQ9RSK9.
SMRiQ9RSK9. Positions 4-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RSK9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiENOG4108UZ0. Bacteria.
COG0200. LUCA.
HOGENOMiHOG000231262.
InParanoidiQ9RSK9.
KOiK02876.
OMAiHKGQWAR.
OrthoDBiEOG6CGCM5.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR030878. Ribosomal_L15.
IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L27A. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RSK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLHDLKPTP GSRKDRKRVG RGPGGTDKTA GRGHKGQKSR SGAGKGAFFE
60 70 80 90 100
GGRSRLIARL PKRGFNNVGT TYEVVKLSQL QDLEDTTFDR DTLEAYRLVR
110 120 130 140 150
RKNRPVKLLA SGEISRAVTV HVDAASAAAI KAVEAAGGRV VLPEVQTQQD

DAQKAE
Length:156
Mass (Da):16,860
Last modified:May 1, 2000 - v1
Checksum:i04D58FA897437A33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11664.1.
PIRiF75314.
RefSeqiNP_295838.1. NC_001263.1.
WP_010888746.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11664; AAF11664; DR_2115.
GeneIDi1797297.
KEGGidra:DR_2115.
PATRICi21631906. VBIDeiRad64572_2338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11664.1.
PIRiF75314.
RefSeqiNP_295838.1. NC_001263.1.
WP_010888746.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-J68-145[»]
1NKWX-ray3.10J1-156[»]
1NWXX-ray3.50J1-156[»]
1NWYX-ray3.30J1-156[»]
1SM1X-ray3.42J1-156[»]
1XBPX-ray3.50J1-156[»]
2ZJPX-ray3.70I1-156[»]
2ZJQX-ray3.30I1-156[»]
2ZJRX-ray2.91I1-156[»]
3CF5X-ray3.30I1-156[»]
3DLLX-ray3.50I1-156[»]
3PIOX-ray3.25I1-156[»]
3PIPX-ray3.45I1-156[»]
4IO9X-ray3.20I1-156[»]
4IOAX-ray3.20I1-156[»]
4IOCX-ray3.60I1-156[»]
4U67X-ray3.65I1-156[»]
4V49X-ray8.70J4-144[»]
4V4AX-ray9.50J4-144[»]
4V4GX-ray11.50M4-144[»]
4WFNX-ray3.54I1-156[»]
5DM6X-ray2.90I4-144[»]
5DM7X-ray3.00I4-144[»]
ProteinModelPortaliQ9RSK9.
SMRiQ9RSK9. Positions 4-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_2115.

Proteomic databases

PRIDEiQ9RSK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11664; AAF11664; DR_2115.
GeneIDi1797297.
KEGGidra:DR_2115.
PATRICi21631906. VBIDeiRad64572_2338.

Phylogenomic databases

eggNOGiENOG4108UZ0. Bacteria.
COG0200. LUCA.
HOGENOMiHOG000231262.
InParanoidiQ9RSK9.
KOiK02876.
OMAiHKGQWAR.
OrthoDBiEOG6CGCM5.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2158-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RSK9.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR030878. Ribosomal_L15.
IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L27A. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  2. "High resolution structure of the large ribosomal subunit from a mesophilic eubacterium."
    Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I., Bartels H., Franceschi F., Yonath A.
    Cell 107:679-688(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, PROTEIN SEQUENCE OF 1-5.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  3. "Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria."
    Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R., Yonath A., Franceschi F.
    Nature 413:814-821(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  4. "Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression."
    Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R., Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E., Kessler M., Yonath A.
    Mol. Cell 11:91-102(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TRNA MIMICS.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  5. "Structural basis for the antibiotic activity of ketolides and azalides."
    Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H., Zarivach R., Yonath A.
    Structure 11:329-338(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH MODIFIED MACROLIDE ANTIBIOTICS.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  6. "Structural insight into the role of the ribosomal tunnel in cellular regulation."
    Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D., Yonath A.
    Nat. Struct. Biol. 10:366-370(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TROLEANDOMYCIN.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  7. "Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin."
    Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A.
    BMC Biol. 2:4-4(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  8. "Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin."
    Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M.
    Mol. Microbiol. 54:1287-1294(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TIAMULIN.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiRL15_DEIRA
AccessioniPrimary (citable) accession number: Q9RSK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 104 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

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.