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Protein

50S ribosomal protein L24

Gene

rplX

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 two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.By similarity
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (TF) when it is bound to the ribosome; this contact may expose a hydrophobic crevice in TF (PubMed:16271892).1 Publication

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

BioCyciDRAD243230:GH46-332-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L24
Gene namesi
Name:rplX
Ordered Locus Names:DR_0322
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
Chaini1 – 11511550S ribosomal protein L24PRO_0000130653Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts trigger factor when it is bound to the ribosome (PubMed:16271892).7 Publications

Protein-protein interaction databases

STRINGi243230.DR_0322.

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Turni8 – 114Combined sources
Beta strandi20 – 234Combined sources
Beta strandi26 – 294Combined sources
Beta strandi33 – 408Combined sources
Turni41 – 444Combined sources
Beta strandi45 – 517Combined sources
Beta strandi52 – 565Combined sources
Beta strandi62 – 643Combined sources
Beta strandi69 – 735Combined sources
Beta strandi78 – 825Combined sources
Beta strandi84 – 896Combined sources
Beta strandi108 – 1103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-S2-115[»]
1NKWX-ray3.10S1-115[»]
1NWXX-ray3.50S1-115[»]
1NWYX-ray3.30S1-115[»]
1SM1X-ray3.42S1-115[»]
1XBPX-ray3.50S1-115[»]
2D3OX-ray3.35S1-115[»]
2ZJPX-ray3.70R1-115[»]
2ZJQX-ray3.30R1-115[»]
2ZJRX-ray2.91R1-115[»]
3CF5X-ray3.30R1-115[»]
3DLLX-ray3.50R1-115[»]
3PIOX-ray3.25R1-115[»]
3PIPX-ray3.45R1-115[»]
4IO9X-ray3.20R1-115[»]
4IOAX-ray3.20R1-115[»]
4IOCX-ray3.60R1-115[»]
4V49X-ray8.70S2-114[»]
4V4AX-ray9.50S2-114[»]
4V4GX-ray11.50V2-114[»]
ProteinModelPortaliQ9RXJ1.
SMRiQ9RXJ1. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RXJ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L24P family.Curated

Phylogenomic databases

eggNOGiCOG0198.
HOGENOMiHOG000039891.
InParanoidiQ9RXJ1.
KOiK02895.
OMAiDIEAPIH.
OrthoDBiEOG6FFSDM.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RXJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRPSAGSHH NDKLHFKKGD TVIVLSGKHK GQTGKVLLAL PRDQKVVVEG
60 70 80 90 100
VNVITKNVKP SMTNPQGGQE QRELALHASK VALVDPETGK ATRVRKQIVD
110
GKKVRVAVAS GKTID
Length:115
Mass (Da):12,358
Last modified:May 1, 2000 - v1
Checksum:iFE0A0ABC51477BE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09903.1.
PIRiB75535.
RefSeqiNP_294045.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF09903; AAF09903; DR_0322.
GeneIDi1798682.
KEGGidra:DR_0322.
PATRICi21628142. VBIDeiRad64572_0488.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09903.1.
PIRiB75535.
RefSeqiNP_294045.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GS2model-S2-115[»]
1NKWX-ray3.10S1-115[»]
1NWXX-ray3.50S1-115[»]
1NWYX-ray3.30S1-115[»]
1SM1X-ray3.42S1-115[»]
1XBPX-ray3.50S1-115[»]
2D3OX-ray3.35S1-115[»]
2ZJPX-ray3.70R1-115[»]
2ZJQX-ray3.30R1-115[»]
2ZJRX-ray2.91R1-115[»]
3CF5X-ray3.30R1-115[»]
3DLLX-ray3.50R1-115[»]
3PIOX-ray3.25R1-115[»]
3PIPX-ray3.45R1-115[»]
4IO9X-ray3.20R1-115[»]
4IOAX-ray3.20R1-115[»]
4IOCX-ray3.60R1-115[»]
4V49X-ray8.70S2-114[»]
4V4AX-ray9.50S2-114[»]
4V4GX-ray11.50V2-114[»]
ProteinModelPortaliQ9RXJ1.
SMRiQ9RXJ1. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF09903; AAF09903; DR_0322.
GeneIDi1798682.
KEGGidra:DR_0322.
PATRICi21628142. VBIDeiRad64572_0488.

Phylogenomic databases

eggNOGiCOG0198.
HOGENOMiHOG000039891.
InParanoidiQ9RXJ1.
KOiK02895.
OMAiDIEAPIH.
OrthoDBiEOG6FFSDM.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-332-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RXJ1.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 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 1-5, X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
    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. "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 nameiRL24_DEIRA
AccessioniPrimary (citable) accession number: Q9RXJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 94 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.