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Q9RXK0

- RL23_DEIRA

UniProt

Q9RXK0 - RL23_DEIRA

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Protein
50S ribosomal protein L23
Gene
rplW, DR_0313
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - 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 (1 Publication and 1 Publication).UniRule annotation

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. rRNA binding Source: UniProtKB-HAMAP
  3. structural constituent of ribosome Source: InterPro
Complete GO annotation...

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

BioCyciDRAD243230:GH46-323-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L23
Gene namesi
Name:rplW
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: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 959450S ribosomal protein L23UniRule annotation
PRO_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 (1 Publication and 1 Publication).9 Publications

Protein-protein interaction databases

STRINGi243230.DR_0313.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-R2-94[»]
1NKWX-ray3.10R1-95[»]
1NWXX-ray3.50R2-95[»]
1NWYX-ray3.30R2-95[»]
1PNUX-ray8.70R2-94[»]
1PNYX-ray9.50R2-94[»]
1SM1X-ray3.42R1-95[»]
1VORX-ray11.50U2-94[»]
1VOUX-ray11.50U2-94[»]
1VP0X-ray11.50U2-94[»]
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[»]
ProteinModelPortaliQ9RXK0.
SMRiQ9RXK0. Positions 2-94.

Miscellaneous databases

EvolutionaryTraceiQ9RXK0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0089.
HOGENOMiHOG000231366.
KOiK02892.
OMAiGKTKRMG.
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

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF09894.1 .
PIRi A75534.
RefSeqi NP_294036.1. NC_001263.1.
WP_010886958.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GS2 model - R 2-94 [» ]
1NKW X-ray 3.10 R 1-95 [» ]
1NWX X-ray 3.50 R 2-95 [» ]
1NWY X-ray 3.30 R 2-95 [» ]
1PNU X-ray 8.70 R 2-94 [» ]
1PNY X-ray 9.50 R 2-94 [» ]
1SM1 X-ray 3.42 R 1-95 [» ]
1VOR X-ray 11.50 U 2-94 [» ]
1VOU X-ray 11.50 U 2-94 [» ]
1VP0 X-ray 11.50 U 2-94 [» ]
1XBP X-ray 3.50 R 2-95 [» ]
2AAR X-ray 3.50 R 1-95 [» ]
2D3O X-ray 3.35 R 1-95 [» ]
2ZJP X-ray 3.70 Q 1-95 [» ]
2ZJQ X-ray 3.30 Q 1-95 [» ]
2ZJR X-ray 2.91 Q 1-95 [» ]
3CF5 X-ray 3.30 Q 1-95 [» ]
3DLL X-ray 3.50 Q 1-95 [» ]
3PIO X-ray 3.25 Q 1-95 [» ]
3PIP X-ray 3.45 Q 1-95 [» ]
4IO9 X-ray 3.20 Q 1-95 [» ]
4IOA X-ray 3.20 Q 1-95 [» ]
4IOC X-ray 3.60 Q 1-95 [» ]
ProteinModelPortali Q9RXK0.
SMRi Q9RXK0. Positions 2-94.
ModBasei Search...

Protein-protein interaction databases

STRINGi 243230.DR_0313.

Proteomic databases

PRIDEi Q9RXK0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF09894 ; AAF09894 ; DR_0313 .
GeneIDi 1799376.
KEGGi dra:DR_0313.
PATRICi 21628124. VBIDeiRad64572_0479.

Phylogenomic databases

eggNOGi COG0089.
HOGENOMi HOG000231366.
KOi K02892.
OMAi GKTKRMG.
OrthoDBi EOG6HTP4P.

Enzyme and pathway databases

BioCyci DRAD243230:GH46-323-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9RXK0.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
HAMAPi MF_01369_B. Ribosomal_L23_B.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view ]
Pfami PF00276. Ribosomal_L23. 1 hit.
[Graphical view ]
SUPFAMi SSF54189. SSF54189. 1 hit.
PROSITEi PS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 95 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

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