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Protein

50S ribosomal protein L23

Gene

rplW

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

One of the early assembly protein (By similarity) it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Forms the main docking site for trigger factor binding to the ribosome (PubMed:16091460 and PubMed:16271892).By similarity2 Publications

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:GH46-323-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L23UniRule annotation
Gene namesi
Name:rplWUniRule annotation
Ordered Locus Names:DR_0313
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
ProteomesiUP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 959450S ribosomal protein L23PRO_0000129406Add
BLAST

Proteomic databases

PRIDEiQ9RXK0.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor when it is bound to the ribosome (PubMed:16091460 and PubMed:16271892).UniRule annotation8 Publications

Protein-protein interaction databases

STRINGi243230.DR_0313.

Structurei

Secondary structure

1
95
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi14 – 207Combined sources
Turni21 – 233Combined sources
Beta strandi26 – 294Combined sources
Helixi35 – 4612Combined sources
Beta strandi51 – 555Combined sources
Beta strandi64 – 674Combined sources
Beta strandi75 – 817Combined sources
Turni91 – 933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-R2-94[»]
1NKWX-ray3.10R1-95[»]
1NWXX-ray3.50R2-95[»]
1NWYX-ray3.30R2-95[»]
1SM1X-ray3.42R1-95[»]
1XBPX-ray3.50R2-95[»]
2AARX-ray3.50R1-95[»]
2D3OX-ray3.35R1-95[»]
2ZJPX-ray3.70Q1-95[»]
2ZJQX-ray3.30Q1-95[»]
2ZJRX-ray2.91Q1-95[»]
3CF5X-ray3.30Q1-95[»]
3DLLX-ray3.50Q1-95[»]
3PIOX-ray3.25Q1-95[»]
3PIPX-ray3.45Q1-95[»]
4IO9X-ray3.20Q1-95[»]
4IOAX-ray3.20Q1-95[»]
4IOCX-ray3.60Q1-95[»]
4V49X-ray8.70R2-94[»]
4V4AX-ray9.50R2-94[»]
4V4GX-ray11.50U2-94[»]
ProteinModelPortaliQ9RXK0.
SMRiQ9RXK0. Positions 2-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RXK0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L23P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0089.
HOGENOMiHOG000231366.
InParanoidiQ9RXK0.
KOiK02892.
OMAiKGIVGRQ.
OrthoDBiEOG6HTP4P.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_01369_B. Ribosomal_L23_B.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]
PfamiPF00276. Ribosomal_L23. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9RXK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHYDILQAP VISEKAYSAM ERGVYSFWVS PKATKTEIKD AIQQAFGVRV
60 70 80 90
IGISTMNVPG KRKRVGRFIG QRNDRKKAIV RLAEGQSIEA LAGQA
Length:95
Mass (Da):10,522
Last modified:January 23, 2007 - v3
Checksum:i09D8AA73699D6046
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09894.1.
PIRiA75534.
RefSeqiNP_294036.1. NC_001263.1.
WP_010886958.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF09894; AAF09894; DR_0313.
GeneIDi1799376.
KEGGidra:DR_0313.
PATRICi21628124. VBIDeiRad64572_0479.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09894.1.
PIRiA75534.
RefSeqiNP_294036.1. NC_001263.1.
WP_010886958.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-R2-94[»]
1NKWX-ray3.10R1-95[»]
1NWXX-ray3.50R2-95[»]
1NWYX-ray3.30R2-95[»]
1SM1X-ray3.42R1-95[»]
1XBPX-ray3.50R2-95[»]
2AARX-ray3.50R1-95[»]
2D3OX-ray3.35R1-95[»]
2ZJPX-ray3.70Q1-95[»]
2ZJQX-ray3.30Q1-95[»]
2ZJRX-ray2.91Q1-95[»]
3CF5X-ray3.30Q1-95[»]
3DLLX-ray3.50Q1-95[»]
3PIOX-ray3.25Q1-95[»]
3PIPX-ray3.45Q1-95[»]
4IO9X-ray3.20Q1-95[»]
4IOAX-ray3.20Q1-95[»]
4IOCX-ray3.60Q1-95[»]
4V49X-ray8.70R2-94[»]
4V4AX-ray9.50R2-94[»]
4V4GX-ray11.50U2-94[»]
ProteinModelPortaliQ9RXK0.
SMRiQ9RXK0. Positions 2-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0313.

Proteomic databases

PRIDEiQ9RXK0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF09894; AAF09894; DR_0313.
GeneIDi1799376.
KEGGidra:DR_0313.
PATRICi21628124. VBIDeiRad64572_0479.

Phylogenomic databases

eggNOGiCOG0089.
HOGENOMiHOG000231366.
InParanoidiQ9RXK0.
KOiK02892.
OMAiKGIVGRQ.
OrthoDBiEOG6HTP4P.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-323-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RXK0.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_01369_B. Ribosomal_L23_B.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]
PfamiPF00276. Ribosomal_L23. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00050. RIBOSOMAL_L23. 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: PROTEIN SEQUENCE OF 2-6, X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, CONTACTS WITH 23S RRNA, CONTACTS WITH L29.
    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.
  9. "Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action."
    Baram D., Pyetan E., Sittner A., Auerbach-Nevo T., Bashan A., Yonath A.
    Proc. Natl. Acad. Sci. U.S.A. 102:12017-12022(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TRIGGER FACTOR.
  10. "The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction."
    Schluenzen F., Wilson D.N., Tian P., Harms J.M., McInnes S.J., Hansen H.A.S., Albrecht R., Buerger J., Wilbanks S.M., Fucini P.
    Structure 13:1685-1694(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TRIGGER FACTOR.

Entry informationi

Entry nameiRL23_DEIRA
AccessioniPrimary (citable) accession number: Q9RXK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 102 of the entry and version 3 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.