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Protein

50S ribosomal protein L22

Gene

rplV

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

This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).By similarity
The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.

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:GH46-326-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L22
Gene namesi
Name:rplV
Ordered Locus Names:DR_0316
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 – 13413450S ribosomal protein L22PRO_0000125151Add
BLAST

Proteomic databases

PRIDEiQ9RXJ7.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L32.6 Publications

Protein-protein interaction databases

STRINGi243230.DR_0316.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 177Combined sources
Beta strandi25 – 339Combined sources
Helixi35 – 4511Combined sources
Beta strandi46 – 494Combined sources
Helixi51 – 566Combined sources
Helixi57 – 593Combined sources
Beta strandi62 – 643Combined sources
Helixi65 – 7915Combined sources
Turni80 – 834Combined sources
Helixi87 – 893Combined sources
Beta strandi90 – 9910Combined sources
Beta strandi103 – 1086Combined sources
Helixi110 – 1123Combined sources
Beta strandi114 – 1196Combined sources
Beta strandi122 – 1309Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J5AX-ray3.50L1-134[»]
1JZXX-ray3.10L1-134[»]
1JZYX-ray3.50L1-134[»]
1JZZX-ray3.80L1-134[»]
1K01X-ray3.50L1-134[»]
1NKWX-ray3.10Q1-134[»]
1NWXX-ray3.50Q1-134[»]
1NWYX-ray3.30Q1-134[»]
1ONDX-ray3.40Q1-134[»]
1SM1X-ray3.42Q1-134[»]
1XBPX-ray3.50Q1-134[»]
2ZJPX-ray3.70P1-134[»]
2ZJQX-ray3.30P1-134[»]
2ZJRX-ray2.91P1-134[»]
3CF5X-ray3.30P1-134[»]
3DLLX-ray3.50P1-134[»]
3PIOX-ray3.25P1-134[»]
3PIPX-ray3.45P1-134[»]
4IO9X-ray3.20P1-134[»]
4IOAX-ray3.20P1-134[»]
4IOCX-ray3.60P1-134[»]
4U67X-ray3.65P1-134[»]
4V49X-ray8.70Q5-134[»]
4V4AX-ray9.50Q5-134[»]
4V4GX-ray11.50T5-134[»]
4WFNX-ray3.54P1-134[»]
5DM6X-ray2.90P8-134[»]
5DM7X-ray3.00P8-134[»]
ProteinModelPortaliQ9RXJ7.
SMRiQ9RXJ7. Positions 5-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RXJ7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22P family.Curated

Phylogenomic databases

eggNOGiENOG4105KAP. Bacteria.
COG0091. LUCA.
HOGENOMiHOG000205046.
InParanoidiQ9RXJ7.
KOiK02890.
OMAiMKRIQPR.
OrthoDBiEOG6V4GKB.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_B. Ribosomal_L22_B.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01044. rplV_bact. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RXJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPEQTFRN KKQRKQQVKL RKPGFAVAKY VRMSPRKVRL VVDVIRGKSV
60 70 80 90 100
QDAEDLLRFI PRSASEPVAK VLNSAKANAL HNDEMLEDRL FVKEAYVDAG
110 120 130
PTLKRLIPRA RGSANIIKKR TSHITIIVAE KGNK
Length:134
Mass (Da):15,159
Last modified:May 1, 2000 - v1
Checksum:i1AE12FA2D59FE944
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09897.1.
PIRiD75534.
RefSeqiNP_294039.1. NC_001263.1.
WP_010886961.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF09897; AAF09897; DR_0316.
GeneIDi1800108.
KEGGidra:DR_0316.
PATRICi21628130. VBIDeiRad64572_0482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09897.1.
PIRiD75534.
RefSeqiNP_294039.1. NC_001263.1.
WP_010886961.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J5AX-ray3.50L1-134[»]
1JZXX-ray3.10L1-134[»]
1JZYX-ray3.50L1-134[»]
1JZZX-ray3.80L1-134[»]
1K01X-ray3.50L1-134[»]
1NKWX-ray3.10Q1-134[»]
1NWXX-ray3.50Q1-134[»]
1NWYX-ray3.30Q1-134[»]
1ONDX-ray3.40Q1-134[»]
1SM1X-ray3.42Q1-134[»]
1XBPX-ray3.50Q1-134[»]
2ZJPX-ray3.70P1-134[»]
2ZJQX-ray3.30P1-134[»]
2ZJRX-ray2.91P1-134[»]
3CF5X-ray3.30P1-134[»]
3DLLX-ray3.50P1-134[»]
3PIOX-ray3.25P1-134[»]
3PIPX-ray3.45P1-134[»]
4IO9X-ray3.20P1-134[»]
4IOAX-ray3.20P1-134[»]
4IOCX-ray3.60P1-134[»]
4U67X-ray3.65P1-134[»]
4V49X-ray8.70Q5-134[»]
4V4AX-ray9.50Q5-134[»]
4V4GX-ray11.50T5-134[»]
4WFNX-ray3.54P1-134[»]
5DM6X-ray2.90P8-134[»]
5DM7X-ray3.00P8-134[»]
ProteinModelPortaliQ9RXJ7.
SMRiQ9RXJ7. Positions 5-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0316.

Proteomic databases

PRIDEiQ9RXJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF09897; AAF09897; DR_0316.
GeneIDi1800108.
KEGGidra:DR_0316.
PATRICi21628130. VBIDeiRad64572_0482.

Phylogenomic databases

eggNOGiENOG4105KAP. Bacteria.
COG0091. LUCA.
HOGENOMiHOG000205046.
InParanoidiQ9RXJ7.
KOiK02890.
OMAiMKRIQPR.
OrthoDBiEOG6V4GKB.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-326-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RXJ7.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_B. Ribosomal_L22_B.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01044. rplV_bact. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 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 nameiRL22_DEIRA
AccessioniPrimary (citable) accession number: Q9RXJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 100 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.